4I9A
Crystal Structure of Sus scrofa Quinolinate Phosphoribosyltransferase in Complex with Nicotinate Mononucleotide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0000166 | molecular_function | nucleotide binding |
| 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 |
| B | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE NCN A 301 |
| Chain | Residue |
| A | ARG138 |
| A | GLY249 |
| A | GLY250 |
| A | SER268 |
| A | LEU269 |
| A | GLY270 |
| A | LYS139 |
| A | HIS160 |
| A | ARG161 |
| A | LYS171 |
| A | GLU201 |
| A | ASP222 |
| A | GLU246 |
| A | SER248 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE NCN B 301 |
| Chain | Residue |
| B | ARG138 |
| B | LYS139 |
| B | HIS160 |
| B | ARG161 |
| B | LYS171 |
| B | GLU201 |
| B | ASP222 |
| B | SER248 |
| B | GLY249 |
| B | LEU269 |
| B | GLY270 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Region: {"description":"Important for hexamer formation","evidences":[{"source":"UniProtKB","id":"Q15274","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q15274","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23626766","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4I9A","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
