4IZU
The E41Q mutant of the amidase from Nesterenkonia sp. AN1 showing the result of Michael addition of acrylamide at the active site cysteine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004040 | molecular_function | amidase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0033388 | biological_process | putrescine biosynthetic process from arginine |
A | 0043864 | molecular_function | indoleacetamide hydrolase activity |
A | 0050126 | molecular_function | N-carbamoylputrescine amidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ROP A 301 |
Chain | Residue |
A | CYS53 |
A | PRO89 |
A | ALA121 |
A | ALA122 |
A | HOH560 |
A | HOH562 |
A | HOH689 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ROP A 302 |
Chain | Residue |
A | LYS111 |
A | TYR115 |
A | GLU119 |
A | CYS145 |
A | TYR146 |
A | ALA170 |
A | HOH708 |
A | GLN41 |
A | TYR47 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE 1HC A 303 |
Chain | Residue |
A | GLN16 |
A | ALA64 |
A | ARG67 |
A | HOH446 |