1QAP
QUINOLINIC ACID PHOSPHORIBOSYLTRANSFERASE WITH BOUND QUINOLINIC ACID
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 | 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 | 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NTM A 300 |
| Chain | Residue |
| A | THR151 |
| A | ARG152 |
| A | LYS153 |
| A | HIS174 |
| A | ARG175 |
| A | GLU256 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE NTM B 301 |
| Chain | Residue |
| B | LYS153 |
| B | HIS174 |
| B | ARG175 |
| B | LEU183 |
| B | GLU256 |
| B | SER258 |
| A | ARG118 |
| B | THR151 |
| B | ARG152 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | THR119 | |
| B | ASN236 | |
| B | GLY259 | |
| B | GLY280 | |
| A | GLU186 | |
| A | VAL215 | |
| A | ASN236 | |
| A | GLY259 | |
| A | GLY280 | |
| B | THR119 | |
| B | GLU186 | |
| B | VAL215 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ARG152 | |
| B | ARG152 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:9016724 |
| Chain | Residue | Details |
| A | LEU176 | |
| B | LEU176 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Blocked amino end (Pro) |
| Chain | Residue | Details |
| A | PRO2 | |
| B | PRO2 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1qpr |
| Chain | Residue | Details |
| A | ARG118 | |
| B | GLU214 | |
| B | ASP235 | |
| B | LYS153 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1qpr |
| Chain | Residue | Details |
| A | GLU214 | |
| A | ASP235 | |
| A | LYS153 | |
| B | ARG118 |
