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 | 8 |
| Details | binding site for residue CVF A 301 |
| Chain | Residue |
| A | ASP101 |
| A | ILE102 |
| A | TYR117 |
| A | ARG250 |
| A | HOH425 |
| A | HOH513 |
| A | HOH520 |
| B | HOH598 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| A | ALA65 |
| A | PHE66 |
| A | PRO217 |
| A | HOH401 |
| A | HOH410 |
| A | HOH446 |
| A | GLN64 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CVF B 301 |
| Chain | Residue |
| B | ASP101 |
| B | ILE102 |
| B | ARG250 |
| B | HOH414 |
| B | HOH454 |
| B | HOH534 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue CVF C 301 |
| Chain | Residue |
| C | SER70 |
| C | ASP101 |
| C | ILE102 |
| C | SER118 |
| C | THR209 |
| C | GLY210 |
| C | TYR211 |
| C | ARG250 |
| C | HOH402 |
| C | HOH409 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue CVF D 301 |
| Chain | Residue |
| D | SER70 |
| D | ASP101 |
| D | SER118 |
| D | THR209 |
| D | GLY210 |
| D | TYR211 |
| D | ARG250 |
| D | HOH408 |
| D | HOH441 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue EDO D 302 |
| Chain | Residue |
| D | ASP229 |
| D | HOH407 |
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 | |
