Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008658 | molecular_function | penicillin binding |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0017001 | biological_process | antibiotic catabolic process |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0008658 | molecular_function | penicillin binding |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
| B | 0046677 | biological_process | response to antibiotic |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0008658 | molecular_function | penicillin binding |
| C | 0008800 | molecular_function | beta-lactamase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0017001 | biological_process | antibiotic catabolic process |
| C | 0046677 | biological_process | response to antibiotic |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0008658 | molecular_function | penicillin binding |
| D | 0008800 | molecular_function | beta-lactamase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0017001 | biological_process | antibiotic catabolic process |
| D | 0046677 | biological_process | response to antibiotic |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue VBC A 301 |
| Chain | Residue |
| A | THR209 |
| A | ARG250 |
| A | HOH407 |
| A | HOH416 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue VBC B 301 |
| Chain | Residue |
| B | HOH452 |
| B | SER118 |
| B | THR209 |
| B | ARG250 |
| B | HOH419 |
| B | HOH429 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue CL C 301 |
| Chain | Residue |
| B | ARG206 |
| C | ARG206 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue VBC C 302 |
| Chain | Residue |
| C | THR209 |
| C | TYR211 |
| C | ARG250 |
| C | HOH401 |
| C | HOH453 |
| C | HOH511 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue VBC D 301 |
| Chain | Residue |
| D | SER118 |
| D | THR209 |
| D | GLY210 |
| D | ARG250 |
| D | HOH410 |
| D | HOH427 |
| D | HOH433 |
| D | HOH542 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue CL D 302 |
| Chain | Residue |
| A | ARG206 |
| D | ARG206 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue EDO D 303 |
| Chain | Residue |
| A | GLU89 |
| A | HIS90 |
| A | ILE112 |
| A | GLN193 |
| A | HOH410 |
| A | HOH482 |
| D | TYR177 |
| D | EDO304 |
| D | HOH402 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 304 |
| Chain | Residue |
| D | TYR177 |
| D | GLU227 |
| D | VAL232 |
| D | EDO303 |
| D | HOH404 |
Functional Information from PROSITE/UniProt
| site_id | PS00337 |
| Number of Residues | 11 |
| Details | BETA_LACTAMASE_D Beta-lactamase class-D active site. PaSTFKIPnSL |
| Chain | Residue | Details |
| A | PRO68-LEU78 | |
