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1JE0

CRYSTAL STRUCTURE OF 5'-DEOXY-5'-METHYLTHIOADENOSINE PHOSPHORYLASE COMPLEXED WITH PHOSPHATE AND TRIS MOLECULE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005829cellular_componentcytosol
A0009116biological_processnucleoside metabolic process
A0009164biological_processnucleoside catabolic process
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0017061molecular_functionS-methyl-5-thioadenosine phosphorylase activity
B0003824molecular_functioncatalytic activity
B0005829cellular_componentcytosol
B0009116biological_processnucleoside metabolic process
B0009164biological_processnucleoside catabolic process
B0016757molecular_functionglycosyltransferase activity
B0016763molecular_functionpentosyltransferase activity
B0017061molecular_functionS-methyl-5-thioadenosine phosphorylase activity
C0003824molecular_functioncatalytic activity
C0005829cellular_componentcytosol
C0009116biological_processnucleoside metabolic process
C0009164biological_processnucleoside catabolic process
C0016757molecular_functionglycosyltransferase activity
C0016763molecular_functionpentosyltransferase activity
C0017061molecular_functionS-methyl-5-thioadenosine phosphorylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 250
ChainResidue
AGLY21
AARG25
AARG43
AARG86
AGLY88
ATHR89
ATRS270
AHOH283

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 B 255
ChainResidue
BARG25
BARG86
BGLY88
BTHR89
BTRS275
BHOH288
CARG43
BGLY21

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 C 260
ChainResidue
BARG43
CGLY21
CARG25
CARG86
CGLY88
CTHR89
CTRS280
CHOH289

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE TRS A 270
ChainResidue
AHIS5
AARG86
ATHR89
AGLU180
AMET181
AGLU182
APO4250

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE TRS B 275
ChainResidue
BARG86
BTHR89
BGLU180
BMET181
BGLU182
BPO4255
CHIS5

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE TRS C 280
ChainResidue
BHIS5
CARG86
CTHR89
CGLU180
CMET181
CGLU182
CPO4260

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: BINDING => ECO:0000269|PubMed:11489901
ChainResidueDetails
AHIS5
BHIS5
CHIS5

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: in other chain => ECO:0000269|PubMed:11489901, ECO:0007744|PDB:1JDS, ECO:0007744|PDB:1JE0
ChainResidueDetails
AGLY21
AARG25
AARG86
BGLY21
BARG25
BARG86
CGLY21
CARG25
CARG86

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:11489901, ECO:0007744|PDB:1JE0
ChainResidueDetails
AARG43
BARG43
CARG43

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: in other chain => ECO:0000269|PubMed:11489901
ChainResidueDetails
AGLU163
ASER204
BGLU163
BSER204
CGLU163
CSER204

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: in other chain => ECO:0000269|PubMed:11489901, ECO:0007744|PDB:1JDT, ECO:0007744|PDB:1JE1
ChainResidueDetails
AGLU180
BGLU180
CGLU180

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

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PDB entries from 2024-07-24

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