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2Q3B

1.8 A Resolution Crystal Structure of O-Acetylserine Sulfhydrylase (OASS) Holoenzyme From MYCOBACTERIUM TUBERCULOSIS

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
A0016740molecular_functiontransferase activity
A0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
A0019344biological_processcysteine biosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
A0080146molecular_functionL-cysteine desulfhydrase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 400
ChainResidue
ATHR71
AGLY73
ATHR75
AGLN144
AMPD404
AHOH566

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MPD A 401
ChainResidue
AGLY296
ALEU300
AHOH414
AHOH421
AALA252
AARG253
AVAL263

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MPD A 402
ChainResidue
AGLU146
AHOH507

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD A 403
ChainResidue
AGLN57
AGLN276
AARG279
AHOH520

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MPD A 404
ChainResidue
ALLP44
AGLN144
AGLY178
AGLY222
AALA225
ACL400
AHOH443
AHOH606

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 Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:17567578
ChainResidueDetails
AASN74
AGLY178
ASER266

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:17567578
ChainResidueDetails
ALLP44

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

224004

PDB entries from 2024-08-21

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