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2Q3C

2.1 A Resolution Crystal Structure of O-Acetylserine Sulfhydrylase (OASS) Holoenzyme From MYCOBACTERIUM TUBERCULOSIS in Complex with the Inhibitory Peptide DFSI

Functional Information from GO Data
ChainGOidnamespacecontents
A0004124molecular_functioncysteine synthase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006535biological_processcysteine biosynthetic process from serine
A0008652biological_processamino acid biosynthetic process
A0016740molecular_functiontransferase activity
A0019344biological_processcysteine biosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
A0080146molecular_functionL-cysteine desulfhydrase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MPD A 311
ChainResidue
AVAL263
ATYR299
AHOH360

Functional Information from PROSITE/UniProt
site_idPS00901
Number of Residues19
DetailsCYS_SYNTHASE Cysteine synthase/cystathionine beta-synthase P-phosphate attachment site. KlEffn.PAnSVKdRiGvaM
ChainResidueDetails
ALYS33-MET51

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17567578","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"17567578","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oas
ChainResidueDetails
ASER266

244349

PDB entries from 2025-11-05

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