5THW
Crystal structure of Amidase, hydantoinase/carbamoylase family from Burkholderia multivorans
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050538 | molecular_function | N-carbamoyl-L-amino-acid hydrolase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050538 | molecular_function | N-carbamoyl-L-amino-acid hydrolase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050538 | molecular_function | N-carbamoyl-L-amino-acid hydrolase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0050538 | molecular_function | N-carbamoyl-L-amino-acid hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue ZN A 501 |
| Chain | Residue |
| A | HIS96 |
| A | ASP107 |
| A | GLU141 |
| A | HIS203 |
| A | URP503 |
| A | HOH622 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 502 |
| Chain | Residue |
| A | URP503 |
| A | ASP107 |
| A | GLU142 |
| A | HIS395 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | binding site for residue URP A 503 |
| Chain | Residue |
| A | HIS96 |
| A | ASP107 |
| A | GLU141 |
| A | GLU142 |
| A | GLN206 |
| A | GLN226 |
| A | ARG301 |
| A | ALA369 |
| A | GLY370 |
| A | HIS395 |
| A | ZN501 |
| A | ZN502 |
| B | HIS239 |
| B | ASN288 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 501 |
| Chain | Residue |
| B | HIS96 |
| B | ASP107 |
| B | HIS203 |
| B | HOH738 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 502 |
| Chain | Residue |
| A | THR102 |
| B | GLU237 |
| B | HIS283 |
| B | PRO284 |
| B | GLY292 |
| B | ARG293 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 501 |
| Chain | Residue |
| C | HIS96 |
| C | ASP107 |
| C | HIS203 |
| C | URP503 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 502 |
| Chain | Residue |
| C | ASP107 |
| C | GLU142 |
| C | HIS395 |
| C | URP503 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | binding site for residue URP C 503 |
| Chain | Residue |
| C | HIS96 |
| C | ASP107 |
| C | GLU141 |
| C | GLU142 |
| C | GLN206 |
| C | GLN226 |
| C | ARG301 |
| C | ALA369 |
| C | GLY370 |
| C | HIS395 |
| C | ZN501 |
| C | ZN502 |
| D | HIS239 |
| D | ASN288 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 501 |
| Chain | Residue |
| D | HIS96 |
| D | ASP107 |
| D | HIS203 |
| D | HOH636 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 502 |
| Chain | Residue |
| C | THR102 |
| D | GLU237 |
| D | HIS283 |
| D | PRO284 |
| D | GLY292 |
