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1JDV

CRYSTAL STRUCTURE OF 5'-DEOXY-5'-METHYLTHIOADENOSINE PHOSPHORYLASE COMPLEXED WITH ADENOSINE AND SULFATE ION

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
D0003824molecular_functioncatalytic activity
D0005829cellular_componentcytosol
D0009116biological_processnucleoside metabolic process
D0009164biological_processnucleoside catabolic process
D0016757molecular_functionglycosyltransferase activity
D0016763molecular_functionpentosyltransferase activity
D0017061molecular_functionS-methyl-5-thioadenosine phosphorylase activity
E0003824molecular_functioncatalytic activity
E0005829cellular_componentcytosol
E0009116biological_processnucleoside metabolic process
E0009164biological_processnucleoside catabolic process
E0016757molecular_functionglycosyltransferase activity
E0016763molecular_functionpentosyltransferase activity
E0017061molecular_functionS-methyl-5-thioadenosine phosphorylase activity
F0003824molecular_functioncatalytic activity
F0005829cellular_componentcytosol
F0009116biological_processnucleoside metabolic process
F0009164biological_processnucleoside catabolic process
F0016757molecular_functionglycosyltransferase activity
F0016763molecular_functionpentosyltransferase activity
F0017061molecular_functionS-methyl-5-thioadenosine phosphorylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1250
ChainResidue
AGLY21
AARG25
AARG86
AGLY88
ATHR89
AADN1260
DARG43

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 2250
ChainResidue
BARG86
BGLY88
BTHR89
BADN2260
CARG43
BGLY21
BARG25

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 3250
ChainResidue
BARG43
CGLY21
CARG86
CGLY88
CTHR89
CHOH3298

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 D 4250
ChainResidue
AARG43
DGLY21
DARG25
DARG86
DGLY88
DTHR89
DADN3260

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 E 5250
ChainResidue
EGLY21
EARG25
EARG86
EGLY88
ETHR89
EADN4260
FARG43

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 F 6250
ChainResidue
EARG43
FGLY21
FARG86
FGLY88
FTHR89
FHOH6299

site_idAC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADN A 1260
ChainResidue
AARG86
ATHR89
ATHR90
AGLY91
APHE160
AGLU163
AVAL179
AGLU180
AMET181
AGLU182
AASP205
ASO41250
DHIS5

site_idAC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ADN B 2260
ChainResidue
BARG86
BTHR89
BGLY91
BPHE160
BGLU163
BGLU180
BMET181
BGLU182
BASP205
BSO42250
CHIS5

site_idAC9
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADN D 3260
ChainResidue
AHIS5
DARG86
DTHR89
DTHR90
DGLY91
DPHE160
DGLU163
DVAL179
DGLU180
DMET181
DGLU182
DASP205
DSO44250

site_idBC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ADN E 4260
ChainResidue
EARG86
ETHR89
ETHR90
EGLY91
EPHE160
EGLU163
EGLU180
EMET181
EGLU182
EASP205
ESO45250
FHIS5

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 Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:11489901
ChainResidueDetails
AHIS5
BHIS5
CHIS5
DHIS5
EHIS5
FHIS5

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING: in other chain => ECO:0000269|PubMed:11489901, ECO:0007744|PDB:1JDS, ECO:0007744|PDB:1JE0
ChainResidueDetails
CGLY21
CARG25
CARG86
DGLY21
DARG25
DARG86
EGLY21
EARG25
EARG86
FGLY21
FARG25
FARG86
AGLY21
AARG25
BARG25
AARG86
BGLY21
BARG86

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:11489901, ECO:0007744|PDB:1JE0
ChainResidueDetails
AARG43
BARG43
CARG43
DARG43
EARG43
FARG43

site_idSWS_FT_FI4
Number of Residues12
DetailsBINDING: in other chain => ECO:0000269|PubMed:11489901
ChainResidueDetails
DGLU163
DSER204
EGLU163
ESER204
FGLU163
FSER204
ASER204
AGLU163
BGLU163
BSER204
CGLU163
CSER204

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: in other chain => ECO:0000269|PubMed:11489901, ECO:0007744|PDB:1JDT, ECO:0007744|PDB:1JE1
ChainResidueDetails
AGLU180
BGLU180
CGLU180
DGLU180
EGLU180
FGLU180

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PDB entries from 2024-05-15

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