5VIR
Crystal structure of probable nicotinate-nucleotide adenylyltransferase from Mycobacterium abscessus in complex with NADP and compound FOL0091
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0009165 | biological_process | nucleotide biosynthetic process |
| A | 0009435 | biological_process | NAD biosynthetic process |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
| A | 0070566 | molecular_function | adenylyltransferase activity |
| 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 | 0009165 | biological_process | nucleotide biosynthetic process |
| B | 0009435 | biological_process | NAD biosynthetic process |
| 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 | 6 |
| Details | binding site for residue 9CG A 300 |
| Chain | Residue |
| A | TRP184 |
| A | TYR185 |
| A | GLN193 |
| B | SER71 |
| B | ASN72 |
| B | PRO73 |
| site_id | AC2 |
| Number of Residues | 33 |
| Details | binding site for residue NAP A 301 |
| Chain | Residue |
| A | THR15 |
| A | PHE16 |
| A | HIS20 |
| A | HIS23 |
| A | THR44 |
| A | LYS50 |
| A | THR88 |
| A | TYR89 |
| A | THR90 |
| A | PHE108 |
| A | THR110 |
| A | GLY111 |
| A | TRP121 |
| A | GLU122 |
| A | VAL136 |
| A | SER169 |
| A | SER170 |
| A | HOH403 |
| A | HOH419 |
| A | HOH423 |
| A | HOH429 |
| A | HOH431 |
| A | HOH435 |
| A | HOH441 |
| A | HOH442 |
| A | HOH455 |
| A | HOH468 |
| A | HOH478 |
| A | HOH481 |
| B | GLU152 |
| A | MET12 |
| A | GLY13 |
| A | GLY14 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue 9CG B 300 |
| Chain | Residue |
| A | SER71 |
| A | ASN72 |
| A | PRO73 |
| B | TRP184 |
| B | TYR185 |
| B | GLN193 |
| site_id | AC4 |
| Number of Residues | 34 |
| Details | binding site for residue NAP B 301 |
| Chain | Residue |
| B | MET12 |
| B | GLY13 |
| B | GLY14 |
| B | THR15 |
| B | HIS20 |
| B | HIS23 |
| B | THR44 |
| B | TRP48 |
| B | THR88 |
| B | THR90 |
| B | PHE108 |
| B | THR110 |
| B | GLY111 |
| B | ALA114 |
| B | SER117 |
| B | ILE118 |
| B | GLU122 |
| B | VAL136 |
| B | ARG138 |
| B | SER169 |
| B | SER170 |
| B | HOH413 |
| B | HOH424 |
| B | HOH425 |
| B | HOH432 |
| B | HOH438 |
| B | HOH441 |
| B | HOH446 |
| B | HOH457 |
| B | HOH462 |
| B | HOH468 |
| B | HOH486 |
| B | HOH510 |
| B | HOH514 |
