2B7Q
Crystal structure of quinolinic acid phosphoribosyltransferase from Helicobacter pylori with nicotinate mononucleotide
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004514 | molecular_function | nicotinate-nucleotide diphosphorylase (carboxylating) activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0009435 | biological_process | NAD+ biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0016757 | molecular_function | glycosyltransferase activity |
A | 0016763 | molecular_function | pentosyltransferase activity |
A | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
A | 0034213 | biological_process | quinolinate catabolic process |
B | 0004514 | molecular_function | nicotinate-nucleotide diphosphorylase (carboxylating) activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0009435 | biological_process | NAD+ biosynthetic process |
B | 0016740 | molecular_function | transferase activity |
B | 0016757 | molecular_function | glycosyltransferase activity |
B | 0016763 | molecular_function | pentosyltransferase activity |
B | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
B | 0034213 | biological_process | quinolinate catabolic process |
C | 0004514 | molecular_function | nicotinate-nucleotide diphosphorylase (carboxylating) activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0009435 | biological_process | NAD+ biosynthetic process |
C | 0016740 | molecular_function | transferase activity |
C | 0016757 | molecular_function | glycosyltransferase activity |
C | 0016763 | molecular_function | pentosyltransferase activity |
C | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
C | 0034213 | biological_process | quinolinate catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE NCN C 1001 |
Chain | Residue |
C | ARG125 |
C | ALA258 |
C | HIS261 |
C | LYS126 |
C | ARG148 |
C | ASP209 |
C | GLU233 |
C | SER235 |
C | GLY236 |
C | SER255 |
C | GLY257 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE NCN A 1002 |
Chain | Residue |
A | THR124 |
A | ARG125 |
A | ARG148 |
A | MET156 |
A | GLU188 |
A | MET207 |
A | ASP209 |
A | SER235 |
A | GLY257 |
A | ALA258 |
A | HIS261 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE NCN B 1003 |
Chain | Residue |
B | ARG125 |
B | LYS126 |
B | ARG148 |
B | MET156 |
B | MET207 |
B | ASP209 |
B | SER235 |
B | GLY236 |
B | ASN237 |
B | GLY257 |
B | ALA258 |
B | HIS261 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | Binding site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"16419067","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1qpr |
Chain | Residue | Details |
A | ASP209 | |
A | LYS126 | |
A | GLU188 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1qpr |
Chain | Residue | Details |
B | ASP209 | |
B | LYS126 | |
B | GLU188 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1qpr |
Chain | Residue | Details |
C | ASP209 | |
C | LYS126 | |
C | GLU188 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qpr |
Chain | Residue | Details |
A | ARG91 |
site_id | CSA5 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qpr |
Chain | Residue | Details |
B | ARG91 |
site_id | CSA6 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qpr |
Chain | Residue | Details |
C | ARG91 |