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4DAB

Crystal structure of the hexameric purine nucleoside phosphorylase from Bacillus subtilis in complex with hypoxanthine

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
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE HPA A 301
ChainResidue
AGLY92
APHE159
AVAL177
AGLU178
AMET179
AGOL308
AHOH405
AHOH408
AHOH446

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 302
ChainResidue
AASN161
ASER164

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 303
ChainResidue
ALYS56
ALYS56

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 304
ChainResidue
AARG87
AGLY89
ASER90
AHOH522

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 305
ChainResidue
ALYS26
ACYS38
AGLU41

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 306
ChainResidue
AHIS4
AARG43
AMET64
APHE159
AGOL308
AHOH521

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 307
ChainResidue
AGLU30
ATHR31
ATYR32
ALEU33
AGLU34

site_idAC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 308
ChainResidue
AMET64
AARG87
ASER90
ACYS91
AGLU178
AMET179
AGLU180
AHPA301
AACT306
AHOH446
AHOH522

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 Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01627
ChainResidueDetails
AASP203

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P50389
ChainResidueDetails
AHIS4
AARG43

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: in other chain => ECO:0000250|UniProtKB:P50389
ChainResidueDetails
AGLY20
AARG24
AARG87
AGLU178
ASER202

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_01627
ChainResidueDetails
AARG216

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PDB entries from 2025-06-18

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