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5LU0

Crystal structure of H. pylori referent strain in complex with PO4

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
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
C0003824molecular_functioncatalytic activity
C0004731molecular_functionpurine-nucleoside phosphorylase activity
C0005829cellular_componentcytosol
C0006139biological_processnucleobase-containing compound metabolic process
C0006152biological_processpurine nucleoside catabolic process
C0009116biological_processnucleoside metabolic process
C0009164biological_processnucleoside catabolic process
C0016740molecular_functiontransferase activity
C0016757molecular_functionglycosyltransferase activity
C0016763molecular_functionpentosyltransferase activity
D0003824molecular_functioncatalytic activity
D0004731molecular_functionpurine-nucleoside phosphorylase activity
D0005829cellular_componentcytosol
D0006139biological_processnucleobase-containing compound metabolic process
D0006152biological_processpurine nucleoside catabolic process
D0009116biological_processnucleoside metabolic process
D0009164biological_processnucleoside catabolic process
D0016740molecular_functiontransferase activity
D0016757molecular_functionglycosyltransferase activity
D0016763molecular_functionpentosyltransferase activity
E0003824molecular_functioncatalytic activity
E0004731molecular_functionpurine-nucleoside phosphorylase activity
E0005829cellular_componentcytosol
E0006139biological_processnucleobase-containing compound metabolic process
E0006152biological_processpurine nucleoside catabolic process
E0009116biological_processnucleoside metabolic process
E0009164biological_processnucleoside catabolic process
E0016740molecular_functiontransferase activity
E0016757molecular_functionglycosyltransferase activity
E0016763molecular_functionpentosyltransferase activity
F0003824molecular_functioncatalytic activity
F0004731molecular_functionpurine-nucleoside phosphorylase activity
F0005829cellular_componentcytosol
F0006139biological_processnucleobase-containing compound metabolic process
F0006152biological_processpurine nucleoside catabolic process
F0009116biological_processnucleoside metabolic process
F0009164biological_processnucleoside catabolic process
F0016740molecular_functiontransferase activity
F0016757molecular_functionglycosyltransferase activity
F0016763molecular_functionpentosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue PO4 A 301
ChainResidue
ACYS19
AGLY20
AARG24
AARG87
AGLY89
ATHR90
ATRS302
DARG43

site_idAC2
Number of Residues11
Detailsbinding site for residue TRS A 302
ChainResidue
AARG87
ATHR90
APHE159
AGLU179
AMET180
AGLU181
APO4301
AHOH420
DHIS4
DARG43
AMET64

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 303
ChainResidue
ALYS78
AGLU191
AHOH421
DTYR160
DPHE162

site_idAC4
Number of Residues8
Detailsbinding site for residue PO4 B 301
ChainResidue
BCYS19
BGLY20
BARG24
BARG87
BGLY89
BTHR90
BTRS302
EARG43

site_idAC5
Number of Residues12
Detailsbinding site for residue TRS B 302
ChainResidue
BMET64
BARG87
BTHR90
BPHE159
BGLU179
BMET180
BGLU181
BPO4301
BHOH456
BHOH474
EHIS4
EARG43

site_idAC6
Number of Residues6
Detailsbinding site for residue EDO B 303
ChainResidue
BLYS78
BTHR79
BHOH413
CILE207
CTHR208
CEDO303

site_idAC7
Number of Residues4
Detailsbinding site for residue EDO B 304
ChainResidue
BLYS78
BGLU191
CEDO303
ETYR160

site_idAC8
Number of Residues7
Detailsbinding site for residue EDO B 305
ChainResidue
BLEU23
BPRO214
BHOH404
BHOH414
BHOH424
EASN6
EHOH487

site_idAC9
Number of Residues4
Detailsbinding site for residue EDO B 306
ChainResidue
BGLU38
BILE39
BASN41
BHOH454

site_idAD1
Number of Residues5
Detailsbinding site for residue EDO B 307
ChainResidue
BTYR27
BLYS30
BGLU219
BHOH425
BHOH431

site_idAD2
Number of Residues7
Detailsbinding site for residue PO4 C 301
ChainResidue
CGLY20
CARG24
CARG87
CGLY89
CTHR90
CTRS302
FARG43

site_idAD3
Number of Residues12
Detailsbinding site for residue TRS C 302
ChainResidue
CMET64
CARG87
CTHR90
CPHE159
CGLU179
CMET180
CGLU181
CPO4301
CHOH468
CHOH556
FHIS4
FARG43

site_idAD4
Number of Residues6
Detailsbinding site for residue EDO C 303
ChainResidue
BTHR74
BLYS78
BEDO303
BEDO304
CTHR208
ETYR160

site_idAD5
Number of Residues5
Detailsbinding site for residue EDO D 301
ChainResidue
DHOH407
APHE162
AHOH446
DLYS78
DGLU191

site_idAD6
Number of Residues8
Detailsbinding site for residue PO4 E 301
ChainResidue
BARG43
ECYS19
EGLY20
EARG24
EARG87
EGLY89
ETHR90
ETRS302

site_idAD7
Number of Residues9
Detailsbinding site for residue TRS E 302
ChainResidue
EMET64
EARG87
ETHR90
EILE178
EGLU179
EMET180
EGLU181
EPO4301
EHOH407

site_idAD8
Number of Residues5
Detailsbinding site for residue EDO E 303
ChainResidue
BTYR160
BPHE162
BHOH422
ELYS78
EGLU191

site_idAD9
Number of Residues3
Detailsbinding site for residue EDO F 301
ChainResidue
CPHE162
FLYS78
FGLU191

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 Residues6
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_01627","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P50389","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues48
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P50389","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsSite: {"description":"Important for catalytic activity","evidences":[{"source":"HAMAP-Rule","id":"MF_01627","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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