4DMO
Crystal structure of the (BACCR)NAT3 arylamine N-acetyltransferase from Bacillus cereus reveals a unique Cys-His-Glu catalytic triad
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016407 | molecular_function | acetyltransferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0046990 | molecular_function | N-hydroxyarylamine O-acetyltransferase activity |
| B | 0016407 | molecular_function | acetyltransferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0046990 | molecular_function | N-hydroxyarylamine O-acetyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE KH2 A 301 |
| Chain | Residue |
| A | TYR95 |
| A | TRP102 |
| A | THR181 |
| A | LEU182 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE KH2 B 301 |
| Chain | Residue |
| B | TYR95 |
| B | TRP102 |
| B | LEU182 |
| B | HOH437 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE KH2 B 302 |
| Chain | Residue |
| B | GLU16 |
| B | MET155 |
| B | ASN160 |
| B | TYR187 |
| B | GLU189 |
| B | GLU15 |
