NaturalProductMech

Browse · Amino acids and peptides · fellutamide B

fellutamide B

naturalproductmech:mibig-a7c02b2a6d MINTED SEEDED

Grounding review: No 3-star ChEBI entry shares this structure, so the record keeps a content-hashed identifier.
What these status tags mean

Curation status describes a workflow state. SEEDED means the record entered through the source-seeding workflow; it does not imply that no later curation occurred. PROPOSED marks an addition awaiting review; REVIEWED records curator sign-off on identity, structure, filing class and producer claims; DEPRECATED retains a superseded or out-of-scope record. These are workflow decisions, not independently verified human review. Agent-assisted contributions may appear in the record history.

Grounding describes the identifier mapping: EXACT uses an ontology identity asserted by the source; MINTED keeps a local identifier when no defensible ontology identity is available; REVIEW_NEEDED flags an exact structure whose ontology identity needs adjudication. The grounding note retains any unresolved alternatives. These tags do not establish the strength of producer or activity evidence.

Structure

Standard InChIKeyMFXAGCQVWGPEJH-LRSLUSHPSA-N
SMILES[H][C@@](CC(C)C)(NC(=O)[C@]([H])(CCC(N)=O)NC(=O)[C@]([H])(CC(N)=O)NC(=O)C[C@H](O)CCCCCCCCC)C=O
Stereochemistryfully defined
Cross-referencesnpatlas:NPA014580, pubchem:9829143

Filing pathway

Amino acids and peptides — computed by NPClassifier npclassifier.gnps2.org@2026-09-07, which is why it is pinned rather than recomputed. The gene cluster's asserted class is nrps, from MIBiG.

Producer organisms 1

A claim that this taxon makes the compound. The basis says what the evidence addressed — a knockout and a database assertion are not the same claim.

TaxonBasisClusterEvidence
Aspergillus nidulans FGSC A4
NCBITaxon:227321		 SOURCE_ASSERTION mibig:BGC0001399 DOI:10.1016/j.chembiol.2008.03.020

Occurrences 1

Somebody found the compound in this organism and cited it. That is not a claim that the organism makes it, and nothing here promotes one to the other.

TaxonSourceReference
Aspergillus nidulans
NCBITaxon:162425		 LOTUS DOI:10.1021/ACSCHEMBIO.6B00213

Biosynthetic gene clusters 1

AccessionHostLocus evidenceGenome
mibig:BGC0001399 Aspergillus nidulans FGSC A4
NCBITaxon:227321 		CLUSTER_UNSTATED genbank:BN001302.1

A locus claim and a taxon claim are different questions. Heterologous expression settles the first and leaves the second where the isolation report left it.

Mechanism & Biosynthesis Overview

PRODUCERS & OCCURRENCE 1 producer (0 causal) 1 cited occurrence BIOSYNTHETIC LOCUS 1 gene cluster 0 curated pathway steps NATURAL PRODUCT fellutamide B naturalproductmech:mibig-a7c02b2a6d Amino acids and peptides TARGETS & BIOACTIVITY 3 molecular targets 0 bioactivities · 5 graphs

Causal graph — biosynthesis 9 nodes, 7 edges

Partial proposed assembly view from reviewed UniProt annotations. FGSC A4 accessions are verified native reference sequences, not verified assay alleles. Reaction ordering is annotation-derived, not genomic ordering or directly inspected enzymology. Carrier-bound intermediates and detailed catalytic domains are omitted. The tentative auxiliary InpF role is intentionally left unconnected to the main sequence because its mechanistic placement is unresolved. The existing MIBiG-derived product identity is retained, including its leucinal S center; no source correction or full primary stereochemical review is claimed.

SubjectPredicateObjectNotesEvidence
InpC (FGSC A4 native reference) is_proposed_to_participate_in Proposed 3-hydroxydodecanoate activation and loading onto InpB Native-reference database assignment, not a newly inspected experiment on this exact allele.
https://www.uniprot.org/uniprotkb/Q5B7J0/entry
https://www.ncbi.nlm.nih.gov/protein/CBF76048.1
  • reference
    https://www.uniprot.org/uniprotkb/Q5B7J0/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed FGSC A4 inpC/ANIA_03490, taxon227321; entry 91, sequence 1, annotation 2026-09-02. FUNCTION annotation. UniProt FUNCTION proposes acyl-AMP formation and loading onto the InpB carrier. No direct acyl-CoA intermediate is asserted merely because the entry is named an acyl-CoA ligase.
    snippet
    inpC activates 3-hydroxydodecanoic acid
  • reference
    https://www.ncbi.nlm.nih.gov/protein/CBF76048.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Identity only: CBF76048.1, 583 aa, ANIA_03490; complete spliced CDS on BN001302.1:3944773..3946984 (7 exon(s), strand 1), GenPept and UniProt sequences agree, including start/stop. Native FGSC A4 reference, not a verified experimental allele.
InpB (FGSC A4 native reference) is_proposed_to_participate_in Proposed sequential L-Asn and L-Gln incorporation Native-reference database assignment, not a newly inspected experiment on this exact allele.
https://www.uniprot.org/uniprotkb/Q5B7I4/entry
https://www.ncbi.nlm.nih.gov/protein/CBF76036.1
  • reference
    https://www.uniprot.org/uniprotkb/Q5B7I4/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed FGSC A4 inpB/ANIA_03496, taxon227321; entry 128, sequence 1, annotation 2026-09-02. FUNCTION annotation. UniProt FUNCTION describes sequential extension of the carrier-bound lipid. No independently inspected purified-enzyme or substrate-specificity assay is claimed.
    snippet
    sequentially extended with L-Asn and L-Gln
  • reference
    https://www.ncbi.nlm.nih.gov/protein/CBF76036.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Identity only: CBF76036.1, 2326 aa, ANIA_03496; complete spliced CDS on BN001302.1:3924481..3931509 (2 exon(s), strand -1), GenPept and UniProt sequences agree, including start/stop. Native FGSC A4 reference, not a verified experimental allele.
InpA (FGSC A4 native reference) is_proposed_to_participate_in Proposed L-Leu incorporation and reductive product release Native-reference database assignment, not a newly inspected experiment on this exact allele.
https://www.uniprot.org/uniprotkb/Q5B7I5/entry
https://www.ncbi.nlm.nih.gov/protein/CBF76038.1
  • reference
    https://www.uniprot.org/uniprotkb/Q5B7I5/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed FGSC A4 inpA/ANIA_03495, taxon227321; entry 131, sequence 1, annotation 2026-09-02. FUNCTION annotation. UniProt FUNCTION assigns L-Leu incorporation and reductive release of (2S)-fellutamide B. The terminal domain mechanism and experimental construct are not independently verified; no hydrolytic release is asserted.
    snippet
    addition of the third amino acid, L-Leu
  • reference
    https://www.ncbi.nlm.nih.gov/protein/CBF76038.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Identity only: CBF76038.1, 1480 aa, ANIA_03495; complete spliced CDS on BN001302.1:3932343..3936952 (2 exon(s), strand 1), GenPept and UniProt sequences agree, including start/stop. Native FGSC A4 reference, not a verified experimental allele.
InpF (FGSC A4 native reference) is_proposed_to_participate_in Possible auxiliary lipodipeptide release or transfer between InpB and InpA Native-reference database assignment, not a newly inspected experiment on this exact allele.
https://www.uniprot.org/uniprotkb/Q5B7I6/entry
https://www.ncbi.nlm.nih.gov/protein/CBF76040.1
  • reference
    https://www.uniprot.org/uniprotkb/Q5B7I6/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed FGSC A4 inpF/ANIA_03494, taxon227321; entry 94, sequence 1, annotation 2026-09-02. FUNCTION annotation. UniProt says this transfer role might occur. Do not turn it into an obligatory transfer step or a demonstrated biochemical reaction; the annotated disruption reduces, rather than eliminates, fellutamide production.
    snippet
    InpF might be involved in the release and transfer
  • reference
    https://www.ncbi.nlm.nih.gov/protein/CBF76040.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Identity only: CBF76040.1, 437 aa, ANIA_03494; complete spliced CDS on BN001302.1:3937185..3938498 (1 exon(s), strand -1), GenPept and UniProt sequences agree, including start/stop. Native FGSC A4 reference, not a verified experimental allele.
Proposed 3-hydroxydodecanoate activation and loading onto InpB is_proposed_to_lead_to Proposed sequential L-Asn and L-Gln incorporation
https://www.uniprot.org/uniprotkb/Q5B7I4/entry
  • reference
    https://www.uniprot.org/uniprotkb/Q5B7I4/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed FGSC A4 inpB/ANIA_03496, taxon227321; entry 128, sequence 1, annotation 2026-09-02. FUNCTION annotation cites PMID27294372 / DOI10.1021/acschembio.6b00213. The reaction sequence is proposed, not independently inspected biochemical reconstruction. The product node retains this owner's source-defined chemical identity; no primary isomer-level sign-off.
Proposed sequential L-Asn and L-Gln incorporation is_proposed_to_lead_to Proposed L-Leu incorporation and reductive product release
https://www.uniprot.org/uniprotkb/Q5B7I5/entry
  • reference
    https://www.uniprot.org/uniprotkb/Q5B7I5/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed FGSC A4 inpA/ANIA_03495, taxon227321; entry 131, sequence 1, annotation 2026-09-02. FUNCTION annotation cites PMID27294372 / DOI10.1021/acschembio.6b00213. The reaction sequence is proposed, not independently inspected biochemical reconstruction. The product node retains this owner's source-defined chemical identity; no primary isomer-level sign-off.
Proposed L-Leu incorporation and reductive product release is_proposed_to_lead_to fellutamide B (existing MIBiG-derived owner)
https://www.uniprot.org/uniprotkb/Q5B7I5/entry
  • reference
    https://www.uniprot.org/uniprotkb/Q5B7I5/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed FGSC A4 inpA/ANIA_03495, taxon227321; entry 131, sequence 1, annotation 2026-09-02. FUNCTION annotation cites PMID27294372 / DOI10.1021/acschembio.6b00213. The reaction sequence is proposed, not independently inspected biochemical reconstruction. The product node retains this owner's source-defined chemical identity; no primary isomer-level sign-off.

Every edge carries its own citation; an uncited edge is refused by the corpus tests.

Causal graph — biosynthesis 8 nodes, 5 edges

Partial producer-regulation and self-resistance view. Mediation links to the proposed assembly graph are intentionally omitted: ScpR transcriptional control does not by itself prove productive cluster activation. InpD resistance involvement remains tentative and no export substrate is demonstrated. InpE is a producer-resistance subunit, not an adopted inhibited target. The conditional InpE requirement is bounded to one inspected primary abstract; other role assignments are database assertions. Reference sequences do not establish experimental allele identity, quantitative phenotypes, direct promoter contacts or complete proteasome assembly.

SubjectPredicateObjectNotesEvidence
ScpR (FGSC A4 native reference) is_annotated_to_participate_in Control of inpA, inpB and other inp-cluster gene expression Native-reference database assignment, not a newly inspected experiment on this exact allele.
https://www.uniprot.org/uniprotkb/Q5B7I8/entry
https://www.ncbi.nlm.nih.gov/protein/CBF76044.1
  • reference
    https://www.uniprot.org/uniprotkb/Q5B7I8/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed FGSC A4 scpR/ANIA_03492, taxon227321; entry 94, sequence 1, annotation 2026-09-02. FUNCTION annotation. UniProt FUNCTION assigns transcriptional control. This does not establish sufficient fellutamide production from ScpR induction alone, direct promoter binding, or complete cluster activation under all conditions.
    snippet
    controls the expression of the nonribosomal peptide synthases inpA and inpB
  • reference
    https://www.ncbi.nlm.nih.gov/protein/CBF76044.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Identity only: CBF76044.1, 277 aa, ANIA_03492; complete spliced CDS on BN001302.1:3941131..3941964 (1 exon(s), strand -1), GenPept and UniProt sequences agree, including start/stop. Native FGSC A4 reference, not a verified experimental allele.
InpD (FGSC A4 native reference) is_proposed_to_participate_in Possible contribution to producer self-resistance Native-reference database assignment, not a newly inspected experiment on this exact allele.
https://www.uniprot.org/uniprotkb/Q5B7I9/entry
https://www.ncbi.nlm.nih.gov/protein/CBF76046.1
  • reference
    https://www.uniprot.org/uniprotkb/Q5B7I9/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed FGSC A4 inpD/ANIA_03491, taxon227321; entry 102, sequence 1, annotation 2026-09-02. FUNCTION annotation. UniProt proposes a resistance contribution, not demonstrated fellutamide export or cargo specificity. Its DISRUPTION PHENOTYPE annotation reports no effect on fellutamide production; production essentiality is not asserted.
    snippet
    may contribute to fellutamide resistance as well
  • reference
    https://www.ncbi.nlm.nih.gov/protein/CBF76046.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Identity only: CBF76046.1, 517 aa, ANIA_03491; complete spliced CDS on BN001302.1:3942367..3944133 (4 exon(s), strand -1), GenPept and UniProt sequences agree, including start/stop. Native FGSC A4 reference, not a verified experimental allele.
InpE (FGSC A4 native reference) is_annotated_to_participate_in Resistance to internally produced fellutamides Native-reference database assignment, not a newly inspected experiment on this exact allele.
https://www.uniprot.org/uniprotkb/Q5B7I7/entry
https://www.ncbi.nlm.nih.gov/protein/CBF76042.1
  • reference
    https://www.uniprot.org/uniprotkb/Q5B7I7/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed FGSC A4 inpE/ANIA_03493, taxon227321; entry 114, sequence 1, annotation 2026-09-02. FUNCTION annotation. UniProt assigns producer self-resistance to this beta-type proteasome subunit. This is not evidence that InpE is an inhibited bioactivity target, nor a verified assembled proteasome complex.
    snippet
    confers resistance to internally produced fellutamides
  • reference
    https://www.ncbi.nlm.nih.gov/protein/CBF76042.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Identity only: CBF76042.1, 215 aa, ANIA_03493; complete spliced CDS on BN001302.1:3939805..3940513 (2 exon(s), strand -1), GenPept and UniProt sequences agree, including start/stop. Native FGSC A4 reference, not a verified experimental allele.
InpE (FGSC A4 native reference) is_native_reference_for_targeted_gene_in inpE deletion with inp-cluster expression activated Identity mapping only; the native reference is not the deletion allele.
https://www.uniprot.org/uniprotkb/Q5B7I7/entry
https://www.ncbi.nlm.nih.gov/protein/CBF76042.1
  • reference
    https://www.uniprot.org/uniprotkb/Q5B7I7/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed FGSC A4 inpE/ANIA_03493, taxon227321; entry 114, sequence 1, annotation 2026-09-02. Gene identity for the named perturbation only.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/CBF76042.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Identity only: CBF76042.1, 215 aa, ANIA_03493; complete spliced CDS on BN001302.1:3939805..3940513 (2 exon(s), strand -1), GenPept and UniProt sequences agree, including start/stop. Native FGSC A4 reference, not a verified experimental allele.
inpE deletion with inp-cluster expression activated demonstrates_requirement_for InpE-dependent resistance to internally produced fellutamide B
DOI:10.1021/acschembio.6b00213
  • reference
    DOI:10.1021/acschembio.6b00213
    evidence type
    PRIMARY_EXPERIMENT
    retrieved on
    2026-10-12
    snippet
    required for resistance to internally produced fellutamide B
    notes
    Only the author abstract indexed at https://europepmc.org/article/MED/27294372 was inspected. It combines inpE deletion with activation of inp-cluster expression and reports a requirement for resistance to internally produced fellutamide B. Full Methods, strain, alleles, dose, growth measurement and primary chemical stereochemistry remain unverified. This is a conditional producer-resistance result, not a purified binding assay or general drug-susceptibility claim.

Every edge carries its own citation; an uncited edge is refused by the corpus tests.

Causal graph — bioactivity 5 nodes, 5 edges

Partial inhibition and structural-target view, separate from producer biosynthesis and self-resistance. H37Rv PrcA/PrcB are sequence-verified reference examples. The processed tagged structural beta chain is represented separately and left without a misleading canonical identifier. 3KRD names H37Rv but also gives H37Ra accessions A5U4D5/A5U4D6 and MRA_2124/MRA_2125. The H37Ra and H37Rv reference sequences are identical. H37Rv accessions here are deliberately selected native references, not proof of the experimental donor strain. Complex identity has no adopted ontology accession. Abstract-bounded inhibition is distinct from the independent deposited covalent model; no human or yeast target transfer, Ki measurement, microbial growth effect or complete mechanism is asserted.

SubjectPredicateObjectNotesEvidence
fellutamide B (free compound) inhibits M. tuberculosis 20S proteasome core
DOI:10.1016/j.abb.2010.06.009
  • reference
    DOI:10.1016/j.abb.2010.06.009
    evidence type
    PRIMARY_EXPERIMENT
    retrieved on
    2026-10-12
    notes
    Only the author abstract indexed at https://europepmc.org/article/MED/20558127 was inspected. It reports time-dependent M. tuberculosis proteasome inhibition and a co-crystal with fellutamide B. Full Methods, kinetic-assay constructs, substrate conditions and experimental compound preparation were not inspected. No quantitative Ki, strain-specific susceptibility, growth inhibition or downstream killing claim is adopted.
    snippet
    1 inhibits the Mtb proteasome in a single-step binding mechanism
PrcA (H37Rv native reference) is_reference_for_outer_ring_subunit_of M. tuberculosis 20S proteasome core Complex membership only; no direct alpha-subunit drug-binding claim. 3KRD names H37Rv but also gives H37Ra accessions A5U4D5/A5U4D6 and MRA_2124/MRA_2125. The H37Ra and H37Rv reference sequences are identical. H37Rv accessions here are deliberately selected native references, not proof of the experimental donor strain.
https://www.uniprot.org/uniprotkb/P9WHU1/entry
https://www.ncbi.nlm.nih.gov/protein/CCP44884.1
https://www.rcsb.org/structure/3KRD
  • reference
    https://www.uniprot.org/uniprotkb/P9WHU1/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed H37Rv native reference; entry68, sequence1, annotation2026-09-02. SUBUNIT annotation assigns the outer alpha rings.
    snippet
    two outer rings, each composed of seven alpha subunits
  • reference
    https://www.ncbi.nlm.nih.gov/protein/CCP44884.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Identity only: native H37Rv prcA/Rv2109c, taxon83332, 248aa. Complete reverse-strand CDS on AL123456.3:2368983..2369729, GenPept CCP44884.1 and UniProt P9WHU1 agree including start/stop under translation table11. Not a verified kinetic-assay construct.
  • reference
    https://www.rcsb.org/structure/3KRD
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Entity1 polymer sequence is identical to full-length H37Rv PrcA1-248. The deposited complex contains14 alpha and14 beta chains; sequence identity does not resolve the conflicting donor-strain metadata.
PrcB precursor (H37Rv native reference) is_sequence_reference_for 3KRD mature PrcB plus C-terminal 6His Reference-to-construct mapping only, not equivalence of full precursor and processed tagged protein. 3KRD names H37Rv but also gives H37Ra accessions A5U4D5/A5U4D6 and MRA_2124/MRA_2125. The H37Ra and H37Rv reference sequences are identical. H37Rv accessions here are deliberately selected native references, not proof of the experimental donor strain.
https://www.uniprot.org/uniprotkb/P9WHT9/entry
https://www.ncbi.nlm.nih.gov/protein/CCP44885.1
https://www.rcsb.org/structure/3KRD
https://www.uniprot.org/uniprotkb/A5U4D6/entry
  • reference
    https://www.uniprot.org/uniprotkb/P9WHT9/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed H37Rv native reference; entry68, sequence1, annotation2026-09-02. Propeptide1-57; mature chain58-291 with active-site Thr58. Reference precursor is291aa.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/CCP44885.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Identity only: native H37Rv prcB/Rv2110c, taxon83332, 291aa. Complete reverse-strand CDS on AL123456.3:2369726..2370601, GenPept CCP44885.1 and UniProt P9WHT9 agree including start/stop under translation table11. Not a verified kinetic-assay construct.
  • reference
    https://www.rcsb.org/structure/3KRD
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Entity2 is exactly PrcB58-291 followed by HHHHHH,240aa. The deposit marks six expression-tag residues. Native-reference Thr58 corresponds to deposited beta label_seq_id1/auth_seq_id301. This is the deposited structural polymer, not a verified kinetic-assay preparation.
  • reference
    https://www.uniprot.org/uniprotkb/A5U4D6/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    The deposit-linked H37Ra PrcB/MRA_2125 sequence is identical to H37Rv P9WHT9. It is not silently adopted as an experimentally verified H37Ra target.
3KRD mature PrcB plus C-terminal 6His is_catalytic_inner_ring_component_of M. tuberculosis 20S proteasome core
https://www.rcsb.org/structure/3KRD
  • reference
    https://www.rcsb.org/structure/3KRD
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Independent2.50-angstrom deposit:14 beta chains in the assembled core, each bearing a covalent linkage from its first mature Thr OG1 to the ligand terminal LEU C atom. Component identity is structural-dataset evidence, not a full primary-paper read.
fellutamide B (free compound) is_modeled_as_covalent_adduct_with 3KRD mature PrcB plus C-terminal 6His A bound hemiacetal is not the free aldehyde owner and has an additional stereocenter. This edge reports a deposited structural model, not irreversible inhibition, proof of purified-beta-alone activity, or quantitative affinity.
https://www.rcsb.org/structure/3KRD
https://files.rcsb.org/download/3KRD.cif
  • reference
    https://www.rcsb.org/structure/3KRD
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    3KRD stores the ligand as NQL peptide plus HXD lipid. All14 beta-ligand linkages are explicitly deposited as covalent Thr OG1 to ligand terminal C. Alpha-subunit binding is not inferred.
    snippet
    in complex with Fellutamide B
  • reference
    https://files.rcsb.org/download/3KRD.cif
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-12
    notes
    Curator mapping with RDKit2026.03.5: representative ligand chain a retains S/S/S peptide centers and R lipid3-OH geometry. Reversing the modeled hemiacetal to free aldehyde and completing the seven unobserved distal lipid carbons from the deposited dodecanoate identity reproduces owner InChIKey MFXAGCQVWGPEJH-LRSLUSHPSA-N. Only32 of39 ligand heavy atoms are observed in that chain; no complete density, primary stereochemical or experimental preparation sign-off.

Every edge carries its own citation; an uncited edge is refused by the corpus tests.

Causal graph — bioactivity 19 nodes, 21 edges

Partial structural association and target-complex composition view, not a temporal assembly pathway. All14 core-subunit types are represented as reference proteins; only beta1/PRE3, beta2/PUP1 and beta5/PRE2 have deposited drug-contact edges. S288c accessions are deliberately selected reference examples, not proof that the baker's-yeast preparation was S288c. Thirteen UniProt accessions stored in the mmCIF are now deleted; they are not adopted as live identifiers. Matching deposited polymer spans do not prove physical truncation of the purified proteins or complete assay-construct identity. In particular, the deposited PUP1 span ends at251 while the annotated mature chain ends at261; absence from the polymer sequence does not establish engineered deletion. PRE4 initiation remains uncertain. The primary2008 full text was not obtained; independent deposition and reference datasets support these claims. No quantitative inhibition, NGF mechanism, all-subunit binding or complete donor-strain reconstruction is asserted.

SubjectPredicateObjectNotesEvidence
fellutamide B (free compound) is_deposited_in_complex_with S. cerevisiae 20S proteasome core
https://www.rcsb.org/structure/3D29
https://files.rcsb.org/download/3D29.cif
  • reference
    https://www.rcsb.org/structure/3D29
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Independent2.60-angstrom structural deposit3D29 contains two copies of each of14 yeast core-subunit types and six ligand copies. This is structural association, not an adopted quantitative yeast inhibition assay.
    snippet
    Proteasome Inhibition by Fellutamide B
  • reference
    https://files.rcsb.org/download/3D29.cif
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-12
    notes
    Curator mapping with RDKit2026.03.5: all six NQL/HXD ligands have39 modeled heavy atoms and retain S/S/S peptide centers plus R lipid3-OH. Reversing the covalent hemiacetal to the free aldehyde reconstructs owner InChIKey MFXAGCQVWGPEJH-LRSLUSHPSA-N. This is coordinate-based mapping, not independent experimental structure elucidation or density-validation sign-off. The new bound hemiacetal center is not assigned to the free owner.
PRE8 (S288c reference) is_reference_for_component_of S. cerevisiae 20S proteasome core Complex membership only; no direct fellutamide-binding edge is asserted for this subunit.
https://www.uniprot.org/uniprotkb/P23639/entry
https://www.ncbi.nlm.nih.gov/protein/NP_013618.1
https://www.rcsb.org/structure/3D29
  • reference
    https://www.uniprot.org/uniprotkb/P23639/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed PRE8 reference, taxon559292; entry244, sequence1, annotation2026-09-02. Native sequence and core-subunit identity for an explicitly selected reference.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/NP_013618.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Identity only: PRE8, 250aa, taxon559292; complete CDS of RefSeq transcript NM_001182451.1 at [0:753](+), including start/stop, translates to NP_013618.1 and UniProt P23639 under table1. This verifies reference annotations, not the experimental donor, physiological initiation choice or assay allele.
  • reference
    https://www.rcsb.org/structure/3D29
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Entity1, author chainsA/O, deposited polymer250aa exactly matches P23639 residues1-250. The mmCIF references A0A6L1BIF8. S288c accessions are deliberately selected reference examples, not proof that the baker's-yeast preparation was S288c. Thirteen UniProt accessions stored in the mmCIF are now deleted; they are not adopted as live identifiers. Matching deposited polymer spans do not prove physical truncation of the purified proteins or complete assay-construct identity.
PRE9 (S288c reference) is_reference_for_component_of S. cerevisiae 20S proteasome core Complex membership only; no direct fellutamide-binding edge is asserted for this subunit.
https://www.uniprot.org/uniprotkb/P23638/entry
https://www.ncbi.nlm.nih.gov/protein/NP_011651.3
https://www.rcsb.org/structure/3D29
  • reference
    https://www.uniprot.org/uniprotkb/P23638/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed PRE9 reference, taxon559292; entry239, sequence1, annotation2026-09-02. Native sequence and core-subunit identity for an explicitly selected reference.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/NP_011651.3
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Identity only: PRE9, 258aa, taxon559292; complete CDS of RefSeq transcript NM_001181264.3 at [0:777](+), including start/stop, translates to NP_011651.3 and UniProt P23638 under table1. This verifies reference annotations, not the experimental donor, physiological initiation choice or assay allele.
  • reference
    https://www.rcsb.org/structure/3D29
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Entity2, author chainsB/P, deposited polymer244aa exactly matches P23638 residues2-245. The mmCIF references A0A6A5PXC6. S288c accessions are deliberately selected reference examples, not proof that the baker's-yeast preparation was S288c. Thirteen UniProt accessions stored in the mmCIF are now deleted; they are not adopted as live identifiers. Matching deposited polymer spans do not prove physical truncation of the purified proteins or complete assay-construct identity.
PRE6 (S288c reference) is_reference_for_component_of S. cerevisiae 20S proteasome core Complex membership only; no direct fellutamide-binding edge is asserted for this subunit.
https://www.uniprot.org/uniprotkb/P40303/entry
https://www.ncbi.nlm.nih.gov/protein/NP_014604.1
https://www.rcsb.org/structure/3D29
  • reference
    https://www.uniprot.org/uniprotkb/P40303/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed PRE6 reference, taxon559292; entry238, sequence1, annotation2026-09-02. Native sequence and core-subunit identity for an explicitly selected reference.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/NP_014604.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Identity only: PRE6, 254aa, taxon559292; complete CDS of RefSeq transcript NM_001183292.1 at [0:765](+), including start/stop, translates to NP_014604.1 and UniProt P40303 under table1. This verifies reference annotations, not the experimental donor, physiological initiation choice or assay allele.
  • reference
    https://www.rcsb.org/structure/3D29
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Entity3, author chainsC/Q, deposited polymer241aa exactly matches P40303 residues3-243. The mmCIF references A0A6A5Q273. S288c accessions are deliberately selected reference examples, not proof that the baker's-yeast preparation was S288c. Thirteen UniProt accessions stored in the mmCIF are now deleted; they are not adopted as live identifiers. Matching deposited polymer spans do not prove physical truncation of the purified proteins or complete assay-construct identity.
PUP2 (S288c reference) is_reference_for_component_of S. cerevisiae 20S proteasome core Complex membership only; no direct fellutamide-binding edge is asserted for this subunit.
https://www.uniprot.org/uniprotkb/P32379/entry
https://www.ncbi.nlm.nih.gov/protein/NP_011769.1
https://www.rcsb.org/structure/3D29
  • reference
    https://www.uniprot.org/uniprotkb/P32379/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed PUP2 reference, taxon559292; entry242, sequence2, annotation2026-09-02. Native sequence and core-subunit identity for an explicitly selected reference.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/NP_011769.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Identity only: PUP2, 260aa, taxon559292; complete CDS of RefSeq transcript NM_001181382.1 at [0:783](+), including start/stop, translates to NP_011769.1 and UniProt P32379 under table1. This verifies reference annotations, not the experimental donor, physiological initiation choice or assay allele.
  • reference
    https://www.rcsb.org/structure/3D29
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Entity4, author chainsD/R, deposited polymer242aa exactly matches P32379 residues9-250. The mmCIF references A0A6A5PXN2. S288c accessions are deliberately selected reference examples, not proof that the baker's-yeast preparation was S288c. Thirteen UniProt accessions stored in the mmCIF are now deleted; they are not adopted as live identifiers. Matching deposited polymer spans do not prove physical truncation of the purified proteins or complete assay-construct identity.
PRE5 (S288c reference) is_reference_for_component_of S. cerevisiae 20S proteasome core Complex membership only; no direct fellutamide-binding edge is asserted for this subunit.
https://www.uniprot.org/uniprotkb/P40302/entry
https://www.ncbi.nlm.nih.gov/protein/NP_014045.1
https://www.rcsb.org/structure/3D29
  • reference
    https://www.uniprot.org/uniprotkb/P40302/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed PRE5 reference, taxon559292; entry240, sequence1, annotation2026-09-02. Native sequence and core-subunit identity for an explicitly selected reference.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/NP_014045.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Identity only: PRE5, 234aa, taxon559292; complete CDS of RefSeq transcript NM_001182825.1 at [0:705](+), including start/stop, translates to NP_014045.1 and UniProt P40302 under table1. This verifies reference annotations, not the experimental donor, physiological initiation choice or assay allele.
  • reference
    https://www.rcsb.org/structure/3D29
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Entity5, author chainsE/S, deposited polymer233aa exactly matches P40302 residues2-234. The mmCIF references A0A6A5PTH4. S288c accessions are deliberately selected reference examples, not proof that the baker's-yeast preparation was S288c. Thirteen UniProt accessions stored in the mmCIF are now deleted; they are not adopted as live identifiers. Matching deposited polymer spans do not prove physical truncation of the purified proteins or complete assay-construct identity.
PRE10 (S288c reference) is_reference_for_component_of S. cerevisiae 20S proteasome core Complex membership only; no direct fellutamide-binding edge is asserted for this subunit.
https://www.uniprot.org/uniprotkb/P21242/entry
https://www.ncbi.nlm.nih.gov/protein/NP_015007.1
https://www.rcsb.org/structure/3D29
  • reference
    https://www.uniprot.org/uniprotkb/P21242/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed PRE10 reference, taxon559292; entry251, sequence2, annotation2026-09-02. Native sequence and core-subunit identity for an explicitly selected reference.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/NP_015007.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Identity only: PRE10, 288aa, taxon559292; complete CDS of RefSeq transcript NM_001183782.1 at [0:867](+), including start/stop, translates to NP_015007.1 and UniProt P21242 under table1. This verifies reference annotations, not the experimental donor, physiological initiation choice or assay allele.
  • reference
    https://www.rcsb.org/structure/3D29
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Entity6, author chainsF/T, deposited polymer244aa exactly matches P21242 residues5-248. The mmCIF references A0A6A5Q4M4. S288c accessions are deliberately selected reference examples, not proof that the baker's-yeast preparation was S288c. Thirteen UniProt accessions stored in the mmCIF are now deleted; they are not adopted as live identifiers. Matching deposited polymer spans do not prove physical truncation of the purified proteins or complete assay-construct identity.
SCL1 (S288c reference) is_reference_for_component_of S. cerevisiae 20S proteasome core Complex membership only; no direct fellutamide-binding edge is asserted for this subunit.
https://www.uniprot.org/uniprotkb/P21243/entry
https://www.ncbi.nlm.nih.gov/protein/NP_011504.3
https://www.rcsb.org/structure/3D29
  • reference
    https://www.uniprot.org/uniprotkb/P21243/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed SCL1 reference, taxon559292; entry254, sequence1, annotation2026-09-02. Native sequence and core-subunit identity for an explicitly selected reference. Historical sequence cautions concern AAA35020.1; these sequences are not used instead of the matching canonical RefSeq.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/NP_011504.3
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Identity only: SCL1, 252aa, taxon559292; complete CDS of RefSeq transcript NM_001180876.3 at [0:759](+), including start/stop, translates to NP_011504.3 and UniProt P21243 under table1. This verifies reference annotations, not the experimental donor, physiological initiation choice or assay allele.
  • reference
    https://www.rcsb.org/structure/3D29
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Entity7, author chainsG/U, deposited polymer243aa exactly matches P21243 residues10-252. The mmCIF references A0A6A5PYC9. S288c accessions are deliberately selected reference examples, not proof that the baker's-yeast preparation was S288c. Thirteen UniProt accessions stored in the mmCIF are now deleted; they are not adopted as live identifiers. Matching deposited polymer spans do not prove physical truncation of the purified proteins or complete assay-construct identity.
PUP1 (S288c reference) is_sequence_reference_for 3D29 beta2 (PUP1) deposited polymer The native precursor is not the processed structural polymer. The modeled N-terminal Thr1 maps to canonical Thr30; native sequence and modeled span are kept distinct.
https://www.uniprot.org/uniprotkb/P25043/entry
https://www.ncbi.nlm.nih.gov/protein/NP_014800.3
https://www.rcsb.org/structure/3D29
  • reference
    https://www.uniprot.org/uniprotkb/P25043/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed PUP1 reference, taxon559292; entry234, sequence1, annotation2026-09-02. Native sequence and core-subunit identity for an explicitly selected reference.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/NP_014800.3
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Identity only: PUP1, 261aa, taxon559292; complete CDS of RefSeq transcript NM_001183576.3 at [0:786](+), including start/stop, translates to NP_014800.3 and UniProt P25043 under table1. This verifies reference annotations, not the experimental donor, physiological initiation choice or assay allele.
  • reference
    https://www.rcsb.org/structure/3D29
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Entity8, author chainsH/V, deposited polymer222aa exactly matches P25043 residues30-251. The mmCIF references A0A6A5Q449. S288c accessions are deliberately selected reference examples, not proof that the baker's-yeast preparation was S288c. Thirteen UniProt accessions stored in the mmCIF are now deleted; they are not adopted as live identifiers. Matching deposited polymer spans do not prove physical truncation of the purified proteins or complete assay-construct identity.
3D29 beta2 (PUP1) deposited polymer is_catalytic_inner_ring_component_of S. cerevisiae 20S proteasome core
https://www.rcsb.org/structure/3D29
  • reference
    https://www.rcsb.org/structure/3D29
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Author chainsH/V are the two beta2 copies in the yeast core. Each modeled N-terminal Thr OG1 is covalently linked to the terminal ligand LEU C atom.
fellutamide B (free compound) is_modeled_as_covalent_adduct_with 3D29 beta2 (PUP1) deposited polymer The bound hemiacetal is chemically distinct from the free aldehyde and has an additional stereocenter. This edge reports the deposited covalent model only.
https://www.rcsb.org/structure/3D29
https://files.rcsb.org/download/3D29.cif
  • reference
    https://www.rcsb.org/structure/3D29
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Two explicit covalent contacts for author chainsH/V: mature Thr1 OG1 to ligand residue3 LEU C. No isolated-subunit assay, quantitative affinity or irreversible inhibition is implied.
  • reference
    https://files.rcsb.org/download/3D29.cif
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-12
    notes
    Curator mapping with RDKit2026.03.5: all six NQL/HXD ligands have39 modeled heavy atoms and retain S/S/S peptide centers plus R lipid3-OH. Reversing the covalent hemiacetal to the free aldehyde reconstructs owner InChIKey MFXAGCQVWGPEJH-LRSLUSHPSA-N. This is coordinate-based mapping, not independent experimental structure elucidation or density-validation sign-off. The new bound hemiacetal center is not assigned to the free owner.
PUP3 (S288c reference) is_reference_for_component_of S. cerevisiae 20S proteasome core Complex membership only; no direct fellutamide-binding edge is asserted for this subunit.
https://www.uniprot.org/uniprotkb/P25451/entry
https://www.ncbi.nlm.nih.gov/protein/NP_011020.3
https://www.rcsb.org/structure/3D29
  • reference
    https://www.uniprot.org/uniprotkb/P25451/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed PUP3 reference, taxon559292; entry233, sequence1, annotation2026-09-02. Native sequence and core-subunit identity for an explicitly selected reference.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/NP_011020.3
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Identity only: PUP3, 205aa, taxon559292; complete CDS of RefSeq transcript NM_001178985.3 at [0:618](+), including start/stop, translates to NP_011020.3 and UniProt P25451 under table1. This verifies reference annotations, not the experimental donor, physiological initiation choice or assay allele.
  • reference
    https://www.rcsb.org/structure/3D29
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Entity9, author chainsI/W, deposited polymer204aa exactly matches P25451 residues2-205. The mmCIF references A0A6L0YA22. S288c accessions are deliberately selected reference examples, not proof that the baker's-yeast preparation was S288c. Thirteen UniProt accessions stored in the mmCIF are now deleted; they are not adopted as live identifiers. Matching deposited polymer spans do not prove physical truncation of the purified proteins or complete assay-construct identity.
PRE1 (S288c reference) is_reference_for_component_of S. cerevisiae 20S proteasome core Complex membership only; no direct fellutamide-binding edge is asserted for this subunit.
https://www.uniprot.org/uniprotkb/P22141/entry
https://www.ncbi.nlm.nih.gov/protein/NP_010928.1
https://www.rcsb.org/structure/3D29
  • reference
    https://www.uniprot.org/uniprotkb/P22141/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed PRE1 reference, taxon559292; entry244, sequence2, annotation2026-09-02. Native sequence and core-subunit identity for an explicitly selected reference.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/NP_010928.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Identity only: PRE1, 198aa, taxon559292; complete CDS of RefSeq transcript NM_001178903.1 at [0:597](+), including start/stop, translates to NP_010928.1 and UniProt P22141 under table1. This verifies reference annotations, not the experimental donor, physiological initiation choice or assay allele.
  • reference
    https://www.rcsb.org/structure/3D29
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Entity10, author chainsJ/X, deposited polymer198aa exactly matches P22141 residues1-198. The mmCIF references A0A6A5Q0W2. S288c accessions are deliberately selected reference examples, not proof that the baker's-yeast preparation was S288c. Thirteen UniProt accessions stored in the mmCIF are now deleted; they are not adopted as live identifiers. Matching deposited polymer spans do not prove physical truncation of the purified proteins or complete assay-construct identity.
PRE2 (S288c reference) is_sequence_reference_for 3D29 beta5 (PRE2) deposited polymer The native precursor is not the processed structural polymer. The modeled N-terminal Thr1 maps to canonical Thr76; native sequence and modeled span are kept distinct.
https://www.uniprot.org/uniprotkb/P30656/entry
https://www.ncbi.nlm.nih.gov/protein/NP_015428.1
https://www.rcsb.org/structure/3D29
  • reference
    https://www.uniprot.org/uniprotkb/P30656/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed PRE2 reference, taxon559292; entry235, sequence3, annotation2026-09-02. Native sequence and core-subunit identity for an explicitly selected reference. Historical sequence cautions concern CAA82203.1; these sequences are not used instead of the matching canonical RefSeq.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/NP_015428.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Identity only: PRE2, 287aa, taxon559292; complete CDS of RefSeq transcript NM_001184200.1 at [0:864](+), including start/stop, translates to NP_015428.1 and UniProt P30656 under table1. This verifies reference annotations, not the experimental donor, physiological initiation choice or assay allele.
  • reference
    https://www.rcsb.org/structure/3D29
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Entity11, author chainsK/Y, deposited polymer212aa exactly matches P30656 residues76-287. The mmCIF references A0A6A5Q5W3. S288c accessions are deliberately selected reference examples, not proof that the baker's-yeast preparation was S288c. Thirteen UniProt accessions stored in the mmCIF are now deleted; they are not adopted as live identifiers. Matching deposited polymer spans do not prove physical truncation of the purified proteins or complete assay-construct identity.
3D29 beta5 (PRE2) deposited polymer is_catalytic_inner_ring_component_of S. cerevisiae 20S proteasome core
https://www.rcsb.org/structure/3D29
  • reference
    https://www.rcsb.org/structure/3D29
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Author chainsK/Y are the two beta5 copies in the yeast core. Each modeled N-terminal Thr OG1 is covalently linked to the terminal ligand LEU C atom.
fellutamide B (free compound) is_modeled_as_covalent_adduct_with 3D29 beta5 (PRE2) deposited polymer The bound hemiacetal is chemically distinct from the free aldehyde and has an additional stereocenter. This edge reports the deposited covalent model only.
https://www.rcsb.org/structure/3D29
https://files.rcsb.org/download/3D29.cif
  • reference
    https://www.rcsb.org/structure/3D29
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Two explicit covalent contacts for author chainsK/Y: mature Thr1 OG1 to ligand residue3 LEU C. No isolated-subunit assay, quantitative affinity or irreversible inhibition is implied.
  • reference
    https://files.rcsb.org/download/3D29.cif
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-12
    notes
    Curator mapping with RDKit2026.03.5: all six NQL/HXD ligands have39 modeled heavy atoms and retain S/S/S peptide centers plus R lipid3-OH. Reversing the covalent hemiacetal to the free aldehyde reconstructs owner InChIKey MFXAGCQVWGPEJH-LRSLUSHPSA-N. This is coordinate-based mapping, not independent experimental structure elucidation or density-validation sign-off. The new bound hemiacetal center is not assigned to the free owner.
PRE7 (S288c reference) is_reference_for_component_of S. cerevisiae 20S proteasome core Complex membership only; no direct fellutamide-binding edge is asserted for this subunit.
https://www.uniprot.org/uniprotkb/P23724/entry
https://www.ncbi.nlm.nih.gov/protein/NP_009512.1
https://www.rcsb.org/structure/3D29
  • reference
    https://www.uniprot.org/uniprotkb/P23724/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed PRE7 reference, taxon559292; entry244, sequence1, annotation2026-09-02. Native sequence and core-subunit identity for an explicitly selected reference.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/NP_009512.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Identity only: PRE7, 241aa, taxon559292; complete CDS of RefSeq transcript NM_001178281.1 at [0:726](+), including start/stop, translates to NP_009512.1 and UniProt P23724 under table1. This verifies reference annotations, not the experimental donor, physiological initiation choice or assay allele.
  • reference
    https://www.rcsb.org/structure/3D29
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Entity12, author chainsL/Z, deposited polymer222aa exactly matches P23724 residues20-241. The mmCIF references A0A6A5Q0P3. S288c accessions are deliberately selected reference examples, not proof that the baker's-yeast preparation was S288c. Thirteen UniProt accessions stored in the mmCIF are now deleted; they are not adopted as live identifiers. Matching deposited polymer spans do not prove physical truncation of the purified proteins or complete assay-construct identity.
PRE4 (S288c reference) is_reference_for_component_of S. cerevisiae 20S proteasome core Complex membership only; no direct fellutamide-binding edge is asserted for this subunit.
https://www.uniprot.org/uniprotkb/P30657/entry
https://www.ncbi.nlm.nih.gov/protein/NP_116708.1
https://www.rcsb.org/structure/3D29
  • reference
    https://www.uniprot.org/uniprotkb/P30657/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed PRE4 reference, taxon559292; entry235, sequence1, annotation2026-09-02. Native sequence and core-subunit identity for an explicitly selected reference. UniProt leaves initiation at Met1 versus Met31 unresolved; the 266-aa reference is not a resolved physiological initiation claim.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/NP_116708.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Identity only: PRE4, 266aa, taxon559292; complete CDS of RefSeq transcript NM_001180015.1 at [0:801](+), including start/stop, translates to NP_116708.1 and UniProt P30657 under table1. This verifies reference annotations, not the experimental donor, physiological initiation choice or assay allele.
  • reference
    https://www.rcsb.org/structure/3D29
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Entity13, author chainsM/1, deposited polymer233aa exactly matches P30657 residues34-266. The mmCIF references A0A8H8ULD3. S288c accessions are deliberately selected reference examples, not proof that the baker's-yeast preparation was S288c. Thirteen UniProt accessions stored in the mmCIF are now deleted; they are not adopted as live identifiers. Matching deposited polymer spans do not prove physical truncation of the purified proteins or complete assay-construct identity.
PRE3 (S288c reference) is_sequence_reference_for 3D29 beta1 (PRE3) deposited polymer The native precursor is not the processed structural polymer. The modeled N-terminal Thr1 maps to canonical Thr20; native sequence and modeled span are kept distinct.
https://www.uniprot.org/uniprotkb/P38624/entry
https://www.ncbi.nlm.nih.gov/protein/NP_012533.1
https://www.rcsb.org/structure/3D29
  • reference
    https://www.uniprot.org/uniprotkb/P38624/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed PRE3 reference, taxon559292; entry231, sequence2, annotation2026-09-02. Native sequence and core-subunit identity for an explicitly selected reference. Historical sequence cautions concern CAA55591.1, CAA60921.1; these sequences are not used instead of the matching canonical RefSeq.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/NP_012533.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Identity only: PRE3, 215aa, taxon559292; complete CDS of RefSeq transcript NM_001181435.1 at [0:648](+), including start/stop, translates to NP_012533.1 and UniProt P38624 under table1. This verifies reference annotations, not the experimental donor, physiological initiation choice or assay allele.
  • reference
    https://www.rcsb.org/structure/3D29
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Entity14, author chainsN/2, deposited polymer196aa exactly matches P38624 residues20-215. The mmCIF references P38624. S288c accessions are deliberately selected reference examples, not proof that the baker's-yeast preparation was S288c. Thirteen UniProt accessions stored in the mmCIF are now deleted; they are not adopted as live identifiers. Matching deposited polymer spans do not prove physical truncation of the purified proteins or complete assay-construct identity.
3D29 beta1 (PRE3) deposited polymer is_catalytic_inner_ring_component_of S. cerevisiae 20S proteasome core
https://www.rcsb.org/structure/3D29
  • reference
    https://www.rcsb.org/structure/3D29
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Author chainsN/2 are the two beta1 copies in the yeast core. Each modeled N-terminal Thr OG1 is covalently linked to the terminal ligand LEU C atom.
fellutamide B (free compound) is_modeled_as_covalent_adduct_with 3D29 beta1 (PRE3) deposited polymer The bound hemiacetal is chemically distinct from the free aldehyde and has an additional stereocenter. This edge reports the deposited covalent model only.
https://www.rcsb.org/structure/3D29
https://files.rcsb.org/download/3D29.cif
  • reference
    https://www.rcsb.org/structure/3D29
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Two explicit covalent contacts for author chainsN/2: mature Thr1 OG1 to ligand residue3 LEU C. No isolated-subunit assay, quantitative affinity or irreversible inhibition is implied.
  • reference
    https://files.rcsb.org/download/3D29.cif
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-12
    notes
    Curator mapping with RDKit2026.03.5: all six NQL/HXD ligands have39 modeled heavy atoms and retain S/S/S peptide centers plus R lipid3-OH. Reversing the covalent hemiacetal to the free aldehyde reconstructs owner InChIKey MFXAGCQVWGPEJH-LRSLUSHPSA-N. This is coordinate-based mapping, not independent experimental structure elucidation or density-validation sign-off. The new bound hemiacetal center is not assigned to the free owner.

Every edge carries its own citation; an uncited edge is refused by the corpus tests.

Causal graph — bioactivity 4 nodes, 4 edges

Partial human beta5 inhibition view. The human beta5 assay is supported only by the cached 2010 author abstract. P28074 is the deliberately selected PSMB5 canonical isoform1 reference, not an independently sequenced assay preparation. Isoforms2/3, immunoproteasome beta5i, donor, tissue and exact construct are not resolved or substituted. The abstract-level activity claim is separate from native-reference identity and database-described complex membership. No transfer of the yeast structural adduct, quantitative Ki, exact preparation or downstream NGF phenotype to this graph.

SubjectPredicateObjectNotesEvidence
fellutamide B (free compound) inhibits Human proteasome beta5 active-site activity
DOI:10.1016/j.abb.2010.06.009
  • reference
    DOI:10.1016/j.abb.2010.06.009
    evidence type
    PRIMARY_EXPERIMENT
    retrieved on
    2026-10-12
    notes
    Only the previously inspected author abstract at https://europepmc.org/article/MED/20558127 is used. It explicitly reports time-dependent inhibition of the human proteasome beta5 active site. Full Methods, exact preparation, dose/substrate conditions and kinetic construct remain uninspected. No quantitative affinity, all-beta-subunit inhibition, NGF induction, microbial killing or irreversible inhibition claim is adopted. The human beta5 assay is supported only by the cached 2010 author abstract. P28074 is the deliberately selected PSMB5 canonical isoform1 reference, not an independently sequenced assay preparation. Isoforms2/3, immunoproteasome beta5i, donor, tissue and exact construct are not resolved or substituted.
    snippet
    it inhibits the human proteasome beta5 active site following a two-step mechanism
PSMB5 precursor (human canonical reference) is_reference_for_subunit_responsible_for Human proteasome beta5 active-site activity The human beta5 assay is supported only by the cached 2010 author abstract. P28074 is the deliberately selected PSMB5 canonical isoform1 reference, not an independently sequenced assay preparation. Isoforms2/3, immunoproteasome beta5i, donor, tissue and exact construct are not resolved or substituted.
https://www.uniprot.org/uniprotkb/P28074/entry
https://www.ncbi.nlm.nih.gov/protein/NP_002788.1
  • reference
    https://www.uniprot.org/uniprotkb/P28074/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed PSMB5 reference, taxon9606; entry256, sequence3, annotation2026-09-02. FUNCTION assigns chymotrypsin-like activity within the20S core; propeptide1-59, mature chain60-263 and nucleophileThr60. This is canonical isoform1, not an isolated-precursor activity assay. Historical sequence cautions concern AAP35423.1, BAA06097.1, CAD97956.1; these sequences are not used instead of the matching canonical RefSeq.
    snippet
    Within the 20S core complex, PSMB5 displays a chymotrypsin-like activity
  • reference
    https://www.ncbi.nlm.nih.gov/protein/NP_002788.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Identity only: PSMB5, 263aa, taxon9606; complete CDS of RefSeq transcript NM_002797.5 at [19:811](+), including start/stop, translates to NP_002788.1 and UniProt P28074 under table1. This verifies reference annotations, not the experimental donor, physiological initiation choice or assay allele.
Human proteasome beta5 active-site activity is_catalytic_activity_of Human20S proteasome core
https://www.uniprot.org/uniprotkb/P28074/entry
  • reference
    https://www.uniprot.org/uniprotkb/P28074/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed PSMB5 reference, taxon9606; entry256, sequence3, annotation2026-09-02. FUNCTION places the beta5 catalytic activity within the20S core, not in a free precursor. Historical sequence cautions concern AAP35423.1, BAA06097.1, CAD97956.1; these sequences are not used instead of the matching canonical RefSeq.
PSMB5 precursor (human canonical reference) is_reference_for_component_of Human20S proteasome core
https://www.uniprot.org/uniprotkb/P28074/entry
  • reference
    https://www.uniprot.org/uniprotkb/P28074/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed PSMB5 reference, taxon9606; entry256, sequence3, annotation2026-09-02. SUBUNIT and FUNCTION identify PSMB5 as a core proteasome component. Membership alone is not a compound-binding assay. Historical sequence cautions concern AAP35423.1, BAA06097.1, CAD97956.1; these sequences are not used instead of the matching canonical RefSeq.

Every edge carries its own citation; an uncited edge is refused by the corpus tests.

Molecular targets 3

TargetTarget organismMeasurementEvidence
Mycobacterium tuberculosis 20S proteasome core
PROTEIN_COMPLEX INHIBITS
UniProtKB:P9WHT9

Target identity is the complex, not an isolated beta subunit. The example is deliberately selected H37Rv native PrcB; its mature58-291 sequence matches the structural beta chain before the6His tag. PrcA is only a complex component in the graph, not a direct binding-target example. 3KRD names H37Rv but also gives H37Ra accessions A5U4D5/A5U4D6 and MRA_2124/MRA_2125. The H37Ra and H37Rv reference sequences are identical. H37Rv accessions here are deliberately selected native references, not proof of the experimental donor strain. Species-level target scope follows the abstract, not a verified H37Rv kinetic assay. No measurement adopted.

 Mycobacterium tuberculosis
NCBITaxon:1773
DOI:10.1016/j.abb.2010.06.009
https://www.uniprot.org/uniprotkb/P9WHT9/entry
https://www.rcsb.org/structure/3KRD
  • reference
    DOI:10.1016/j.abb.2010.06.009
    evidence type
    PRIMARY_EXPERIMENT
    retrieved on
    2026-10-12
    notes
    Only the author abstract indexed at https://europepmc.org/article/MED/20558127 was inspected. It reports time-dependent M. tuberculosis proteasome inhibition and a co-crystal with fellutamide B. Full Methods, kinetic-assay constructs, substrate conditions and experimental compound preparation were not inspected. No quantitative Ki, strain-specific susceptibility, growth inhibition or downstream killing claim is adopted.
  • reference
    https://www.uniprot.org/uniprotkb/P9WHT9/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed H37Rv native reference; entry68, sequence1, annotation2026-09-02. ACTIVITY REGULATION annotates fellutamide B inhibition of proteasome activity, not isolated precursor inhibition.
    snippet
    Proteasome activity is potently inhibited by fellutamide B
  • reference
    https://www.rcsb.org/structure/3KRD
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Structural corroboration and construct mapping only: entity2 is the processed beta sequence plus6His. Conflicting strain identifiers remain unresolved.
Saccharomyces cerevisiae 20S proteasome core
PROTEIN_COMPLEX BINDS
UniProtKB:P38624, UniProtKB:P25043, UniProtKB:P30656

Structural-model binding only: six covalent ligand contacts across the beta1,beta2,beta5 copies. The remaining11 subunit types are complex members, not adopted direct-binding examples. S288c accessions are deliberately selected reference examples, not proof that the baker's-yeast preparation was S288c. Thirteen UniProt accessions stored in the mmCIF are now deleted; they are not adopted as live identifiers. Matching deposited polymer spans do not prove physical truncation of the purified proteins or complete assay-construct identity. No quantitative inhibition measurement or irreversible-binding claim.

 Saccharomyces cerevisiae
NCBITaxon:4932
https://www.rcsb.org/structure/3D29
https://files.rcsb.org/download/3D29.cif
  • reference
    https://www.rcsb.org/structure/3D29
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    3D29 explicit covalent contacts at author chainsH/V,K/Y,N/2. UniProt examples map the canonical precursors to their deposited processed polymer spans.
  • reference
    https://files.rcsb.org/download/3D29.cif
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-12
    notes
    Curator mapping with RDKit2026.03.5: all six NQL/HXD ligands have39 modeled heavy atoms and retain S/S/S peptide centers plus R lipid3-OH. Reversing the covalent hemiacetal to the free aldehyde reconstructs owner InChIKey MFXAGCQVWGPEJH-LRSLUSHPSA-N. This is coordinate-based mapping, not independent experimental structure elucidation or density-validation sign-off. The new bound hemiacetal center is not assigned to the free owner.
Human20S proteasome beta5 activity
PROTEIN_COMPLEX INHIBITS
UniProtKB:P28074

The human beta5 assay is supported only by the cached 2010 author abstract. P28074 is the deliberately selected PSMB5 canonical isoform1 reference, not an independently sequenced assay preparation. Isoforms2/3, immunoproteasome beta5i, donor, tissue and exact construct are not resolved or substituted. Target scope is beta5 activity within the complex, not all proteasome sites or an isolated precursor. No quantitative measurement adopted.

 Homo sapiens
NCBITaxon:9606
DOI:10.1016/j.abb.2010.06.009
https://www.uniprot.org/uniprotkb/P28074/entry
https://www.ncbi.nlm.nih.gov/protein/NP_002788.1
  • reference
    DOI:10.1016/j.abb.2010.06.009
    evidence type
    PRIMARY_EXPERIMENT
    retrieved on
    2026-10-12
    notes
    Only the previously inspected author abstract at https://europepmc.org/article/MED/20558127 is used. It explicitly reports time-dependent inhibition of the human proteasome beta5 active site. Full Methods, exact preparation, dose/substrate conditions and kinetic construct remain uninspected. No quantitative affinity, all-beta-subunit inhibition, NGF induction, microbial killing or irreversible inhibition claim is adopted. The human beta5 assay is supported only by the cached 2010 author abstract. P28074 is the deliberately selected PSMB5 canonical isoform1 reference, not an independently sequenced assay preparation. Isoforms2/3, immunoproteasome beta5i, donor, tissue and exact construct are not resolved or substituted.
  • reference
    https://www.uniprot.org/uniprotkb/P28074/entry
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Reviewed PSMB5 reference, taxon9606; entry256, sequence3, annotation2026-09-02. Canonical reference for the beta5 component, with mature chain60-263; other isoforms and beta5i are not selected. Historical sequence cautions concern AAP35423.1, BAA06097.1, CAD97956.1; these sequences are not used instead of the matching canonical RefSeq.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/NP_002788.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-12
    notes
    Identity only: PSMB5, 263aa, taxon9606; complete CDS of RefSeq transcript NM_002797.5 at [19:811](+), including start/stop, translates to NP_002788.1 and UniProt P28074 under table1. This verifies reference annotations, not the experimental donor, physiological initiation choice or assay allele.

Explore across X-Mech

AntibioticMech (fellutamide B) ↗ MediaIngredientMech (naturalproductmech:mibig-a7c02b2a6d) ↗ TaxonMech: Aspergillus nidulans FGSC A4 (NCBITaxon:227321) ↗ PathwayMech (mibig:BGC0001399) ↗

Open questions 3

curator-fellutamide-b-assembly-and-assay-scope — Which direct assays resolve InpF transfer, InpD transport, terminal release chemistry and exact experimental alleles?

curator-fellutamide-b-proteasome-strain-and-construct — Which donor strain and exact kinetic construct were used, and how should the conflicting3KRD strain metadata be resolved?

curator-fellutamide-b-eukaryotic-reference-and-assay-scope — Which experimental donor strains, complete preparations and human isoforms were used, and how should PRE4 initiation and inactive deposit references be resolved?

Provenance

Source conceptSourceVersion
BGC0001399MIBIG4

This page is generated from data/natural_products/amino_acids_and_peptides/fellutamide-b.yaml, which is generated from the committed inventories. Neither is edited by hand.