2II1
Crystal structure of Acetamidase (10172637) from Bacillus Halodurans at 1.95 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 400 |
| Chain | Residue |
| A | ASN154 |
| A | ASP156 |
| A | ASP181 |
| A | CA401 |
| A | HOH442 |
| A | HOH514 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 401 |
| Chain | Residue |
| A | GLU197 |
| A | CA400 |
| A | HOH514 |
| A | CYS36 |
| A | ASP181 |
| A | HIS183 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 400 |
| Chain | Residue |
| B | ASN154 |
| B | ASP156 |
| B | ASP181 |
| B | CA401 |
| B | HOH409 |
| B | HOH504 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 401 |
| Chain | Residue |
| B | CYS36 |
| B | ASP181 |
| B | HIS183 |
| B | GLU197 |
| B | CA400 |
| B | HOH504 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA C 400 |
| Chain | Residue |
| C | ASN154 |
| C | ASP156 |
| C | ASP181 |
| C | CA401 |
| C | HOH405 |
| C | HOH488 |
| C | HOH505 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 401 |
| Chain | Residue |
| C | CYS36 |
| C | ASP181 |
| C | HIS183 |
| C | GLU197 |
| C | CA400 |
| C | HOH505 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA D 400 |
| Chain | Residue |
| D | ASN154 |
| D | ASP156 |
| D | ASP181 |
| D | CA401 |
| D | HOH429 |
| D | HOH503 |
| D | HOH518 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 401 |
| Chain | Residue |
| D | CYS36 |
| D | ASP181 |
| D | HIS183 |
| D | GLU197 |
| D | CA400 |
| D | HOH518 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 402 |
| Chain | Residue |
| B | GLY163 |
| B | ASP222 |
| B | HOH421 |
| B | HOH503 |
| C | GLU232 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA D 402 |
| Chain | Residue |
| C | GLU66 |
| C | HOH498 |
| D | ALA250 |
| D | THR253 |
| D | LEU255 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 402 |
| Chain | Residue |
| C | ALA250 |
| C | THR253 |
| C | LEU255 |
| C | HOH429 |
| C | HOH507 |
| D | GLU66 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA C 403 |
| Chain | Residue |
| C | GLU232 |
| C | PRO278 |
| C | HOH407 |
| C | HOH449 |
| C | HOH502 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA C 404 |
| Chain | Residue |
| C | LEU102 |
| C | ASN103 |
| C | HOH457 |
| D | THR49 |
| D | HOH486 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 403 |
| Chain | Residue |
| A | GLU66 |
| A | HOH439 |
| A | HOH475 |
| B | ALA250 |
| B | THR253 |
| B | LEU255 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 404 |
| Chain | Residue |
| A | ALA250 |
| A | THR253 |
| A | LEU255 |
| B | GLU66 |
