4WSO
X-ray crystal structure of a nicotinate nucleotide adenylyltransferase from Burkholderia thailandensis bound to NAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004515 | molecular_function | nicotinate-nucleotide adenylyltransferase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0009435 | biological_process | NAD+ biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
| A | 0070566 | molecular_function | adenylyltransferase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004515 | molecular_function | nicotinate-nucleotide adenylyltransferase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0009435 | biological_process | NAD+ biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
| B | 0070566 | molecular_function | adenylyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 31 |
| Details | binding site for residue NAD A 301 |
| Chain | Residue |
| A | GLY35 |
| A | LYS72 |
| A | THR112 |
| A | TYR113 |
| A | THR114 |
| A | ILE135 |
| A | GLY136 |
| A | ASP138 |
| A | GLN139 |
| A | TRP146 |
| A | ARG147 |
| A | GLY36 |
| A | ARG163 |
| A | LEU205 |
| A | VAL207 |
| A | PO4302 |
| A | HOH452 |
| A | HOH454 |
| A | HOH455 |
| A | HOH457 |
| A | HOH484 |
| A | HOH491 |
| A | THR37 |
| A | HOH494 |
| A | HOH548 |
| A | PHE38 |
| A | HIS42 |
| A | HIS45 |
| A | LEU48 |
| A | TYR70 |
| A | GLN71 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue PO4 A 302 |
| Chain | Residue |
| A | HIS42 |
| A | HIS45 |
| A | ARG163 |
| A | ALA208 |
| A | ALA209 |
| A | NAD301 |
| A | HOH453 |
| A | HOH494 |
| A | HOH496 |
| A | HOH548 |
| A | HOH549 |
| site_id | AC3 |
| Number of Residues | 30 |
| Details | binding site for residue NAD B 301 |
| Chain | Residue |
| B | GLY35 |
| B | GLY36 |
| B | THR37 |
| B | PHE38 |
| B | HIS42 |
| B | HIS45 |
| B | LEU48 |
| B | TYR70 |
| B | GLN71 |
| B | LYS72 |
| B | TYR113 |
| B | THR114 |
| B | ILE135 |
| B | GLY136 |
| B | ASP138 |
| B | GLN139 |
| B | TRP146 |
| B | ARG147 |
| B | ARG163 |
| B | LEU205 |
| B | VAL207 |
| B | PO4302 |
| B | HOH452 |
| B | HOH453 |
| B | HOH454 |
| B | HOH459 |
| B | HOH467 |
| B | HOH470 |
| B | HOH488 |
| B | HOH495 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | binding site for residue PO4 B 302 |
| Chain | Residue |
| B | HIS42 |
| B | HIS45 |
| B | ARG163 |
| B | ALA208 |
| B | ALA209 |
| B | NAD301 |
| B | HOH468 |
| B | HOH470 |
| B | HOH495 |
| B | HOH533 |
| B | HOH534 |
