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sulfanilamide

CHEBI:45373 ·resolve ·ANTIBACTERIAL ·EXACT SEEDED

A sulfonamide in which the sulfamoyl functional group is attached to aniline at the 4-position. — ChEBI

Machine-generated and unreviewed. Identity, structure and cross-references come straight from ChEBI's and CARD's own data; no curator has signed off on this record yet.

Classification

sulfonamide antibioticARO:3000282

Strictly broader compounds or drug classes this molecule belongs to.

Chemical structure

Computed structure properties
Molecular formulaC6H8N2O2S
Charge0
Average mass172.209 Da
Monoisotopic mass172.03065 Da
SourceChEBI
InChIKeyFDDDEECHVMSUSB-UHFFFAOYSA-N

SMILES

Nc1ccc(S(N)(=O)=O)cc1

InChI

InChI=1S/C6H8N2O2S/c7-5-1-3-6(4-2-5)11(8,9)10/h1-4H,7H2,(H2,8,9,10)

Also called

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.

Drug registries

Identifiers that name a drug rather than a structure. One of these can cover a parent compound, its salts and its stereoisomers, which this corpus keeps as separate records, so it is not an equivalence of structure.

Patents and articles

Documents about this compound. A patent covers a class and an article covers a topic; neither identifies a structure.

Activity roles

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

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
SourceNative IDLabelMinted CURIEVersion
ARO ARO:3007468 sulfanilamide antibioticmech:aro-dba3a37e97 2026-08-30
CHEBI CHEBI:45373 sulfanilamide antibioticmech:chebi-fac7578230 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.

Carbonic anhydrase PROTEIN MEASURED_TARGET_ASSOCIATION

BindingDB quantitative measurement in the named target organism; source assay descriptions and identifiers are retained per measurement. Evidence status: PRIMARY_EVIDENCE. Source: BINDINGDB 2026-09 (retrieved 2026-08-31).

Mycobacterium tuberculosis CAS/NITR204 NCBITaxon:1310114

Quantitative measurements
TypeReported valueAssayBindingDB IDsReference
KI 7110 nM CA Inhibition Assay
An Applied Photophysics stopped-flow instrument has been used for assaying the CA-catalyzed CO2 hydration activity. Phenol red has been used as indicator, working at the absorbance maximum of 557 nm. The inhibition constants were obtained by nonlinear least-squares methods. The IC50 was obtained by using curve-fitting algorithm, and Ki values were calculated by using the Cheng-Prusoff equation. The catalytic activity of these enzymes was calculated from Lineweaver-Burk plots, and represent the mean from at least three different determinations.		 RSID 53329
assay 3201_1
monomer 10857		 PMID:19338333
Organism-specific examples
ProteinGeneOrganismEntry
Carbonic anhydrase UniProtKB:R4ML78
BindingDB target chain 1		 — Mycobacterium tuberculosis CAS/NITR204 NCBITaxon:1310114 UNREVIEWED

Carbonic anhydrase PROTEIN MEASURED_TARGET_ASSOCIATION

BindingDB quantitative measurement in the named target organism; source assay descriptions and identifiers are retained per measurement. Evidence status: PRIMARY_EVIDENCE. Source: BINDINGDB 2026-09 (retrieved 2026-08-31).

Cryptococcus neoformans NCBITaxon:5207

Quantitative measurements
TypeReported valueAssayBindingDB IDsReference
KI 765 nM CA Inhibition Assay
An Applied Photophysics stopped-flow instrument has been used for assaying the CA-catalyzed CO2 hydration activity. Phenol red has been used as indicator, working at the absorbance maximum of 557 nm. The inhibition constants were obtained by nonlinear least-squares methods. The IC50 was obtained by using curve-fitting algorithm, and Ki values were calculated by using the Cheng-Prusoff equation. The catalytic activity of these enzymes was calculated from Lineweaver-Burk plots, and represent the mean from at least three different determinations.		 RSID 60910
assay 3445_1
monomer 10857		 PMID:19450983
Organism-specific examples
ProteinGeneOrganismEntry
Carbonic anhydrase UniProtKB:Q3I4V7
BindingDB target chain 1		 — Cryptococcus neoformans NCBITaxon:5207 UNREVIEWED

Siderophore-binding protein PROTEIN MEASURED_TARGET_ASSOCIATION

BindingDB quantitative measurement in the named target organism; source assay descriptions and identifiers are retained per measurement. Evidence status: PRIMARY_EVIDENCE. Source: BINDINGDB 2026-09 (retrieved 2026-08-31).

Mycobacterium tuberculosis NCBITaxon:1773

Quantitative measurements
TypeReported valueAssayBindingDB IDsReference
KI 7.11e+3 nM CA Inhibition Assay
An Applied Photophysics stopped-flow instrument has been used for assaying the CA-catalyzed CO2 hydration activity [Khalifah et al., J. Biol. Chem., 246:2561-2573]. Phenol red (at a concentration of 0.2 mM)has been used as indicator, working at the absorbance maximum of 557 nm with 10-20 mM Hepes (pH 7.5, for α-CAs) or TRIS (pH 8.3 for β-CAs) as buffers, and20 mM Na2SO4 (for α-CAs) or 20 mM NaCl for β-CAs (for maintaining constant the ionic strength), following the initial rates of the CA-catalyzed CO2 hydration reaction for a period of 10-100 s. The CO2 concentrations ranged from 1.7 to 17 mM for the determination of the kinetic parameters and inhibition constants. For each inhibitor, at least six traces of the initial 5-10% of the reaction have been used for determining the initial velocity. The uncatalyzed rates were determined in the same manner and subtracted from the total observed rates. Stock solutions of inhibitor (10 mM) were prepared in distilled deionized water and dilutions up to 0.01 nM were done thereafter with distilled-deionized water. Inhibitor andenzyme solutions were preincubated together for 15 min at room temperature prior to assay in order to allow for the formation of the E-I complex. The inhibition constants were obtained by non-linear least-squares methods using PRISM 3, whereas the kinetic parameters for the uninhibited enzymes from Lineweaver-Burk plots,as reported earlier.		 RSID 417609
assay 8291_1
monomer 10857		 PMID:22299588
Organism-specific examples
ProteinGeneOrganismEntry
Siderophore-binding protein UniProtKB:A0A045J7I4
BindingDB target chain 1		 — Mycobacterium tuberculosis NCBITaxon:1773 UNREVIEWED

Mechanism summary

Clinical status
APPROVED

Curation history

  1. SEEDED_FROM_SOURCES 2026-08-30 · seed_from_sources

    Seeded from data/raw/ inventories (ARO, CHEBI)

  2. RESEEDED_FROM_SOURCES 2026-08-30 · seed_from_sources

    Re-seeded from updated data/raw/ inventories

  3. RESEEDED_FROM_SOURCES 2026-08-30 · seed_from_sources

    Re-seeded from updated data/raw/ inventories

  4. RESEEDED_FROM_SOURCES 2026-08-31 · seed_from_sources

    Re-seeded from updated data/raw/ inventories

  5. RESEEDED_FROM_SOURCES 2026-08-31 · seed_from_sources

    Re-seeded from updated data/raw/ inventories

  6. RESEEDED_FROM_SOURCES 2026-08-31 · seed_from_sources

    Re-seeded from updated data/raw/ inventories

  7. RESEEDED_FROM_SOURCES 2026-09-10 · seed_from_sources

    Re-seeded from updated data/raw/ inventories

Provenance

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

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