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2B7N

Crystal structure of quinolinic acid phosphoribosyltransferase from Helicobacter pylori

Functional Information from GO Data
ChainGOidnamespacecontents
A0004514molecular_functionnicotinate-nucleotide diphosphorylase (carboxylating) activity
A0005737cellular_componentcytoplasm
A0009435biological_processNAD+ biosynthetic process
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0019363biological_processpyridine nucleotide biosynthetic process
A0034213biological_processquinolinate catabolic process
B0004514molecular_functionnicotinate-nucleotide diphosphorylase (carboxylating) activity
B0005737cellular_componentcytoplasm
B0009435biological_processNAD+ biosynthetic process
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0016763molecular_functionpentosyltransferase activity
B0019363biological_processpyridine nucleotide biosynthetic process
B0034213biological_processquinolinate catabolic process
C0004514molecular_functionnicotinate-nucleotide diphosphorylase (carboxylating) activity
C0005737cellular_componentcytoplasm
C0009435biological_processNAD+ biosynthetic process
C0016740molecular_functiontransferase activity
C0016757molecular_functionglycosyltransferase activity
C0016763molecular_functionpentosyltransferase activity
C0019363biological_processpyridine nucleotide biosynthetic process
C0034213biological_processquinolinate catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 2001
ChainResidue
CLYS126
CASN237
CGLY257
CALA258
CHIS261
CHOH2043

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 2002
ChainResidue
BALA258
BHIS261
BHOH2003
BLYS126
BASN237
BGLY257

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 2003
ChainResidue
ALYS126
AASN237
AVAL256
AGLY257
AALA258
AHIS261
AHOH2062

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE NTM A 1001
ChainResidue
ATHR124
AARG125
AHIS147
AARG148
AMET156
AMET207
AGLU233
AHOH2004
AHOH2034
BARG91

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE NTM B 1002
ChainResidue
AARG91
BTHR124
BARG125
BHIS147
BARG148
BMET156
BMET207
BGLU233
BHOH2006
BHOH2072
BHOH2078

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE NTM C 1003
ChainResidue
CARG91
CTHR124
CARG125
CHIS147
CARG148
CMET156
CLYS158
CMET207
CGLU233
CHOH2019

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues18
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16419067","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qpr
ChainResidueDetails
AASP209
ALYS126
AGLU188

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qpr
ChainResidueDetails
BASP209
BLYS126
BGLU188

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qpr
ChainResidueDetails
CASP209
CLYS126
CGLU188

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qpr
ChainResidueDetails
AARG91

site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qpr
ChainResidueDetails
BARG91

site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qpr
ChainResidueDetails
CARG91

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PDB entries from 2025-07-23

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