Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5MX8

Crystal structure of H. pylori purine nucleoside phosphorylase from clinical isolate HpPNP-3

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
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue HPA A 301
ChainResidue
ATHR90
ACYS91
AGLY92
APHE159
AILE178
AGLU179
ASER203
AASP204
AHOH445

site_idAC2
Number of Residues7
Detailsbinding site for residue PO4 A 302
ChainResidue
ACYS19
AGLY20
AARG24
AARG43
AARG87
AGLY89
ATHR90

site_idAC3
Number of Residues6
Detailsbinding site for residue PG4 A 303
ChainResidue
ALYS78
ATYR160
ASER161
APHE162
AGLU191
ALEU192

site_idAC4
Number of Residues7
Detailsbinding site for residue PG4 A 304
ChainResidue
AMET1
ALYS8
ALYS215
AGLU216
AGLU219
APG4306
APG4307

site_idAC5
Number of Residues5
Detailsbinding site for residue PG4 A 305
ChainResidue
AGLU163
AHIS165
AALA166
AGLN172
AHOH420

site_idAC6
Number of Residues5
Detailsbinding site for residue PG4 A 306
ChainResidue
ALYS8
ALYS101
AGLU216
ASER220
APG4304

site_idAC7
Number of Residues8
Detailsbinding site for residue PG4 A 307
ChainResidue
AMET1
AASN6
AALA7
ALEU23
APRO214
AGLU219
APG4304
AHOH476

site_idAC8
Number of Residues6
Detailsbinding site for residue PG4 A 308
ChainResidue
APRO96
AVAL98
AASP102
AASP147
ALYS149
AHIS205

site_idAC9
Number of Residues10
Detailsbinding site for residue PG4 A 309
ChainResidue
ALYS101
AILE103
AILE146
AASP147
ASER201
ASER220
APHE221
AASP222
AASN223
AMET224

site_idAD1
Number of Residues7
Detailsbinding site for residue PG4 A 310
ChainResidue
AASP112
ALYS114
AARG117
AVAL118
AASN122
AHIS123
AGLU163

Functional Information from PROSITE/UniProt
site_idPS01232
Number of Residues16
DetailsPNP_UDP_1 Purine and other phosphorylases family 1 signature. GhGMGiAScTIyvtEL
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
AASP204

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
AGLU179
ASER203

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

221716

PDB entries from 2024-06-26

PDB statisticsPDBj update infoContact PDBjnumon