CHIR-090

CHEBI:134107 ·resolve ·ANTIMICROBIAL_UNSPECIFIED ·EXACT REVIEWED

An L-threonine derivative obtained by formal condensation of the carboxy group of 4-({4-[(morpholin-4-yl)methyl]phenyl}ethynyl)benzoic acid with the amino group of N-hydroxy-L-threoninamide. — ChEBI

Classification

Strictly broader compounds or drug classes this molecule belongs to.

Label unavailable CHEBI:22702
Label unavailable CHEBI:24650
Label unavailable CHEBI:38785
Label unavailable CHEBI:73474
Label unavailable CHEBI:84189

Chemical structure

Computed structure properties
Molecular formula	C24H27N3O5
Charge	0
Average mass	437.496 Da
Monoisotopic mass	437.19507 Da
Source	ChEBI
InChIKey	FQYBTYFKOHPWQT-VGSWGCGISA-N

SMILES

C[C@@H](O)[C@H](NC(=O)c1ccc(C#Cc2ccc(CN3CCOCC3)cc2)cc1)C(=O)NO

InChI

InChI=1S/C24H27N3O5/c1-17(28)22(24(30)26-31)25-23(29)21-10-8-19(9-11-21)3-2-18-4-6-20(7-5-18)16-27-12-14-32-15-13-27/h4-11,17,22,28,31H,12-16H2,1H3,(H,25,29)(H,26,30)/t17-,22+/m1/s1

Also called

N-[(2S,3R)-3-hydroxy-1-(hydroxyamino)-1-oxobutan-2-yl]-4-({4-[(morpholin-4-yl)methyl]phenyl}ethynyl)benzamide (EXACT_SYNONYM)— chebi

Cross-references

Identifiers for this same structure in other resources. An accession that lands on two different structures in this corpus is withheld from both rather than shown here, since it names at most one of them.

reaxys:18777591

Activity roles

Every antimicrobial role a source asserts for this compound — the unreduced evidence behind its antimicrobial_class.

antimicrobial agent CHEBI:33281

Source concepts

Every upstream concept that resolved to this record. The merge is the product: this is what shows ChEBI and CARD are describing the same structure.

Upstream concepts merged into this record
Source	Native ID	Label	Minted CURIE	Version
CHEBI	`CHEBI:134107`	CHIR-090	`antibioticmech:chebi-6da0985f25`	2026-08-30

Molecular targets

The molecular entity or process this compound acts on. Each target carries evidence — this is a mechanistic claim, not a classification.

UDP-3-O-acyl-N-acetylglucosamine deacetylase (LpxC) PROTEIN DIRECT_BINDING_TARGET

A 1.79-angstrom Y. enterocolitica LpxC cocrystal and kinetic analysis showed zinc chelation and two-step slow, tight binding. Evidence status: PRIMARY_EVIDENCE. Source: PRIMARY_LITERATURE 2010-12 (retrieved 2026-09-02).

Yersinia enterocolitica NCBITaxon:630

PMID:21171638 (Primary CHIR-090-bound LpxC structural, kinetic, and antibacterial study (DOI:10.1021/bi101622a).)

Mechanism summary

Mode of action: CELL_MEMBRANE_SYNTHESIS_INHIBITION microbial target — CURATOR: PMID:21171638 measured slow, tight CHIR-090 inhibition of Yersinia enterocolitica LpxC and determined a 1.79-angstrom inhibitor-enzyme structure. Its hydroxamate chelates the active-site zinc and its tail occupies the hydrophobic tunnel, blocking the first committed step in lipid A biosynthesis.

Record-level evidence

PMID:21171638 (Primary CHIR-090 LpxC cocrystal and mechanism study.)

Curation history

SEEDED_FROM_SOURCES 2026-08-30 · seed_from_sources
Seeded from data/raw/ inventories (CHEBI)
RESEEDED_FROM_SOURCES 2026-08-30 · seed_from_sources
Re-seeded from updated data/raw/ inventories
RESEEDED_FROM_SOURCES 2026-08-30 · seed_from_sources
Re-seeded from updated data/raw/ inventories
REVIEWED 2026-09-02 · codex · LLM-assisted
Verified exact ChEBI identity, structure, antibiotic role, and unspecified filing class; added lipid-A-biosynthesis inhibition and the directly bound bacterial LpxC target.

Provenance

Seeded by scripts/seed_from_sources.py from the committed inventories in data/raw/. View the record (YAML).

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