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1OAS

O-ACETYLSERINE SULFHYDRYLASE FROM SALMONELLA TYPHIMURIUM

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004124molecular_functioncysteine synthase activity
A0005737cellular_componentcytoplasm
A0006535biological_processcysteine biosynthetic process from serine
A0008652biological_processamino acid biosynthetic process
A0016740molecular_functiontransferase activity
A0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
A0019344biological_processcysteine biosynthetic process
A0080146molecular_functionL-cysteine desulfhydrase activity
B0003824molecular_functioncatalytic activity
B0004124molecular_functioncysteine synthase activity
B0005737cellular_componentcytoplasm
B0006535biological_processcysteine biosynthetic process from serine
B0008652biological_processamino acid biosynthetic process
B0016740molecular_functiontransferase activity
B0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
B0019344biological_processcysteine biosynthetic process
B0080146molecular_functionL-cysteine desulfhydrase activity
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PLP A 323
ChainResidue
AGLY228
AILE229
ASER272
APRO299
ASER300
ATYR305
AHOH329
AHOH334
AHOH350
AHOH365
ALYS41
AASN71
AGLY174
AGLY176
ATHR177
AGLY178
ATHR180

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE PLP B 323
ChainResidue
BLYS41
BASN71
BGLY174
BVAL175
BGLY176
BTHR177
BGLY178
BGLY179
BTHR180
BGLY228
BILE229
BSER272
BPRO299
BSER300
BTYR305
BHOH335
BHOH338
BHOH339

site_idPLP
Number of Residues2
DetailsSCHIFF-BASE LINKAGE TO COFACTOR
ChainResidue
ALYS41
BLYS41

Functional Information from PROSITE/UniProt
site_idPS00901
Number of Residues19
DetailsCYS_SYNTHASE Cysteine synthase/cystathionine beta-synthase P-phosphate attachment site. KvEsrn.PSfSVKcRiGanM
ChainResidueDetails
ALYS30-MET48

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11023792","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"11023792","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10452898","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11023792","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9761678","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 11170356, 12515544
ChainResidueDetails
ASER272
ALYS41

site_idCSA2
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 11170356, 12515544
ChainResidueDetails
BSER272
BLYS41

site_idMCSA1
Number of Residues2
DetailsM-CSA 865
ChainResidueDetails
ALYS41covalent catalysis, proton shuttle (general acid/base)
ASER272electrostatic stabiliser

site_idMCSA2
Number of Residues2
DetailsM-CSA 865
ChainResidueDetails
BLYS41covalent catalysis, proton shuttle (general acid/base)
BSER272electrostatic stabiliser

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PDB entries from 2025-12-10

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