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4D98

Crystal structure of the hexameric purine nucleoside phosphorylase from Bacillus subtilis in space group H32 at pH 7.5

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004731molecular_functionpurine-nucleoside phosphorylase activity
A0005829cellular_componentcytosol
A0006139biological_processnucleobase-containing compound metabolic process
A0006152biological_processpurine nucleoside catabolic process
A0009116biological_processnucleoside metabolic process
A0009164biological_processnucleoside catabolic process
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0042278biological_processpurine nucleoside metabolic process
B0003824molecular_functioncatalytic activity
B0004731molecular_functionpurine-nucleoside phosphorylase activity
B0005829cellular_componentcytosol
B0006139biological_processnucleobase-containing compound metabolic process
B0006152biological_processpurine nucleoside catabolic process
B0009116biological_processnucleoside metabolic process
B0009164biological_processnucleoside catabolic process
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0016763molecular_functionpentosyltransferase activity
B0042278biological_processpurine nucleoside metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
AGLY20
AARG87
AGLY89
ASER90
AHOH444
AHOH473
AHOH475
AHOH485
BARG43

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 302
ChainResidue
APHE154
AASN161
ASER164
AHOH478

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 301
ChainResidue
AARG43
BGLY20
BARG24
BARG87
BGLY89
BSER90
BHOH478

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 302
ChainResidue
BPHE154
BASN161
BSER164
BHOH485

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 303
ChainResidue
AGLY192
AHOH525
AHOH565
BARG95
BLYS96

Functional Information from PROSITE/UniProt
site_idPS01232
Number of Residues16
DetailsPNP_UDP_1 Purine and other phosphorylases family 1 signature. GtGMGvPSiSIyvnEL
ChainResidueDetails
AGLY61-LEU76

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_01627","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P50389","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P50389","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Important for catalytic activity","evidences":[{"source":"HAMAP-Rule","id":"MF_01627","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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