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3UAZ

Crystal structure of Bacillus cereus adenosine phosphorylase D204N mutant complexed with inosine

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 NOS A 236
ChainResidue
AHIS4
AMET180
AGLU181
AASN204
AILE206
ASO4237
AHOH262
AHOH299
AHOH336
AARG43
AARG87
ATHR90
ACYS91
AGLY92
APHE159
AVAL178
AGLU179

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 237
ChainResidue
AGLY20
AARG43
AARG87
AGLY89
ATHR90
ANOS236
AHOH263
AHOH298

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 238
ChainResidue
ATYR160
AARG161
AGLU162
ATYR173
ALYS191
AHOH242
AHOH364

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 239
ChainResidue
AGLU75
AGLN78
ASER79
ATYR160
AHOH248

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
AASN204

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

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: in other chain => ECO:0000250|UniProtKB:P50389
ChainResidueDetails
AGLY20
AARG24
AARG87
AGLU162
AGLU179
ASER203

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_01627
ChainResidueDetails
AARG217

223790

PDB entries from 2024-08-14

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