4IZT
The E41Q mutant of the amidase from Nesterenkonia sp. AN1 showing covalent addition of the acetamide moiety of fluoroacetamide at the active site cysteine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| A | 0033388 | biological_process | putrescine biosynthetic process from arginine |
| A | 0050126 | molecular_function | N-carbamoylputrescine amidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACM A 301 |
| Chain | Residue |
| A | GLN41 |
| A | TYR47 |
| A | LYS111 |
| A | TYR115 |
| A | GLU119 |
| A | CYS145 |
| A | TYR146 |
| A | FTM303 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FTM A 302 |
| Chain | Residue |
| A | GLU149 |
| A | LEU171 |
| A | TYR115 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FTM A 303 |
| Chain | Residue |
| A | TYR47 |
| A | ALA170 |
| A | LEU171 |
| A | ALA172 |
| A | ACM301 |
