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1JDU

CRYSTAL STRUCTURE OF 5'-DEOXY-5'-METHYLTHIOADENOSINE PHOSPHORYLASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004731molecular_functionpurine-nucleoside phosphorylase activity
A0005829cellular_componentcytosol
A0009116biological_processnucleoside metabolic process
A0009164biological_processnucleoside catabolic process
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0017061molecular_functionS-methyl-5-thioadenosine phosphorylase activity
B0003824molecular_functioncatalytic activity
B0004731molecular_functionpurine-nucleoside phosphorylase activity
B0005829cellular_componentcytosol
B0009116biological_processnucleoside metabolic process
B0009164biological_processnucleoside catabolic process
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0016763molecular_functionpentosyltransferase activity
B0017061molecular_functionS-methyl-5-thioadenosine phosphorylase activity
C0003824molecular_functioncatalytic activity
C0004731molecular_functionpurine-nucleoside phosphorylase activity
C0005829cellular_componentcytosol
C0009116biological_processnucleoside metabolic process
C0009164biological_processnucleoside catabolic process
C0016740molecular_functiontransferase activity
C0016757molecular_functionglycosyltransferase activity
C0016763molecular_functionpentosyltransferase activity
C0017061molecular_functionS-methyl-5-thioadenosine phosphorylase activity
Functional Information from PROSITE/UniProt
site_idPS01232
Number of Residues16
DetailsPNP_UDP_1 Purine and other phosphorylases family 1 signature. ThGIGgPSiAIvleEL
ChainResidueDetails
ATHR61-LEU76

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11489901","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues15
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"11489901","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JDS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1JE0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11489901","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JE0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"11489901","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"11489901","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JDT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1JE1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cg6
ChainResidueDetails
ALEU207
AASP205

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cg6
ChainResidueDetails
BLEU207
BASP205

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cg6
ChainResidueDetails
CLEU207
CASP205

238582

PDB entries from 2025-07-09

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