Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008658 | molecular_function | penicillin binding |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0017001 | biological_process | antibiotic catabolic process |
| B | 0008658 | molecular_function | penicillin binding |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 301 |
| Chain | Residue |
| A | GLU205 |
| A | THR210 |
| A | HOH417 |
| A | HOH444 |
| A | HOH583 |
| B | ARG199 |
| B | TYR212 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| B | ARG122 |
| B | ILE202 |
| B | GLN203 |
| A | ARG199 |
| A | HOH403 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | SER124 |
| A | LYS214 |
| A | THR215 |
| A | GLY216 |
| A | THR217 |
| A | EDO304 |
| A | HOH450 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | PHE108 |
| A | EDO303 |
| A | HOH539 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 305 |
| Chain | Residue |
| A | TYR183 |
| A | LYS198 |
| A | HOH515 |
| B | GLU205 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 301 |
| Chain | Residue |
| A | GLU205 |
| A | HOH416 |
| B | TYR183 |
| B | LYS198 |
Functional Information from PROSITE/UniProt
| site_id | PS00337 |
| Number of Residues | 11 |
| Details | BETA_LACTAMASE_D Beta-lactamase class-D active site. PqSTFKVPnAL |
| Chain | Residue | Details |
| A | PRO74-LEU84 | |
