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4DAE

Crystal structure of the hexameric purine nucleoside phosphorylase from Bacillus subtilis in complex with 6-chloroguanosine

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
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0042278biological_processpurine nucleoside metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 6CR A 301
ChainResidue
AHIS4
AMET179
AGLU180
ASER202
AASP203
AVAL205
ACL302
AHOH431
AHOH459
AARG43
AARG87
ASER90
ACYS91
AGLY92
APHE159
AVAL177
AGLU178

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 302
ChainResidue
AARG87
AGLY89
ASER90
A6CR301
AHOH459

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 303
ChainResidue
ALYS26
AGLU41

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 304
ChainResidue
ASER2
AVAL3
AGLU75
AGLN78
ASER79
ATYR160

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 305
ChainResidue
ACYS128
AALA129
ATYR172
AALA189
AHOH443
AHOH463

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

222624

PDB entries from 2024-07-17

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