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 |
| A | 0071555 | biological_process | cell wall organization |
| 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 |
| B | 0071555 | biological_process | cell wall organization |
| 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 |
| C | 0071555 | biological_process | cell wall organization |
| 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 |
| D | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue XEV A 301 |
| Chain | Residue |
| A | TYR117 |
| A | TYR211 |
| A | ARG250 |
| A | HOH405 |
| A | HOH451 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue XEV B 301 |
| Chain | Residue |
| B | THR209 |
| B | ARG250 |
| B | HOH415 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 302 |
| Chain | Residue |
| B | ASP96 |
| B | HOH418 |
| B | LYS94 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue EDO B 303 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO C 301 |
| Chain | Residue |
| C | THR167 |
| C | ILE170 |
| C | SER171 |
| C | ARG174 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue XEV D 301 |
| Chain | Residue |
| D | TYR117 |
| D | THR209 |
| D | ARG250 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue CL D 302 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO D 303 |
| Chain | Residue |
| D | GLU227 |
| D | ASP229 |
| D | HOH466 |
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 | |
