3C2R
Crystal structure of the quinolinate phosphoribosyl transferase (BNA6) from Sachharomyces cerevisiae complexed with the inhibitor phthalate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004514 | molecular_function | nicotinate-nucleotide diphosphorylase (carboxylating) activity |
| A | 0005634 | cellular_component | nucleus |
| 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 |
| A | 0034354 | biological_process | 'de novo' NAD biosynthetic process from tryptophan |
| B | 0004514 | molecular_function | nicotinate-nucleotide diphosphorylase (carboxylating) activity |
| B | 0005634 | cellular_component | nucleus |
| 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 |
| B | 0034354 | biological_process | 'de novo' NAD biosynthetic process from tryptophan |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PHT A 300 |
| Chain | Residue |
| A | THR142 |
| A | ARG143 |
| A | HIS165 |
| A | ARG166 |
| A | SER256 |
| B | ARG107 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PHT B 301 |
| Chain | Residue |
| B | LYS144 |
| B | HIS165 |
| B | ARG166 |
| B | SER256 |
| A | ARG107 |
| B | THR142 |
| B | ARG143 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18321072 |
| Chain | Residue | Details |
| A | THR108 | |
| A | TYR167 | |
| A | ASP177 | |
| A | ASN228 | |
| B | THR108 | |
| B | TYR167 | |
| B | ASP177 | |
| B | ASN228 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ARG143 | |
| A | GLY257 | |
| B | ARG143 | |
| B | GLY257 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | CYS207 | |
| B | CYS207 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1qpr |
| Chain | Residue | Details |
| A | GLU206 | |
| A | LYS144 | |
| A | ASP227 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1qpr |
| Chain | Residue | Details |
| B | GLU206 | |
| B | LYS144 | |
| B | ASP227 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qpr |
| Chain | Residue | Details |
| A | ARG107 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qpr |
| Chain | Residue | Details |
| B | ARG107 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1qpr |
| Chain | Residue | Details |
| A | GLU204 | |
| A | LYS144 | |
| A | ASP227 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1qpr |
| Chain | Residue | Details |
| B | GLU204 | |
| B | LYS144 | |
| B | ASP227 |
| site_id | MCSA1 |
| Number of Residues | 1 |
| Details | M-CSA 945 |
| Chain | Residue | Details |
| A | THR145 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 1 |
| Details | M-CSA 945 |
| Chain | Residue | Details |
| B | THR145 | electrostatic stabiliser |
