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 | 13 |
| Details | binding site for residue AVM A 301 |
| Chain | Residue |
| A | SER70 |
| A | HOH420 |
| A | HOH445 |
| A | HOH545 |
| A | HOH646 |
| A | KCX73 |
| A | VAL120 |
| A | LEU158 |
| A | THR209 |
| A | ARG214 |
| A | SER244 |
| A | LEU247 |
| A | ARG250 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 302 |
| Chain | Residue |
| A | ARG206 |
| C | ARG206 |
| C | HOH581 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue AVM B 301 |
| Chain | Residue |
| B | SER70 |
| B | KCX73 |
| B | VAL120 |
| B | LEU158 |
| B | THR209 |
| B | TYR211 |
| B | ARG214 |
| B | SER244 |
| B | LEU247 |
| B | ARG250 |
| B | HOH405 |
| B | HOH436 |
| B | HOH485 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | binding site for residue AVM C 301 |
| Chain | Residue |
| C | SER70 |
| C | VAL120 |
| C | THR209 |
| C | TYR211 |
| C | THR213 |
| C | ARG214 |
| C | SER244 |
| C | LEU247 |
| C | ARG250 |
| C | HOH402 |
| C | HOH409 |
| C | HOH437 |
| C | HOH499 |
| C | HOH548 |
| C | HOH550 |
| C | HOH624 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue EDO C 302 |
| Chain | Residue |
| A | ASP229 |
| A | ASP230 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | binding site for residue AVM D 301 |
| Chain | Residue |
| D | SER70 |
| D | VAL120 |
| D | LEU158 |
| D | THR209 |
| D | TYR211 |
| D | ARG214 |
| D | SER244 |
| D | LEU247 |
| D | ARG250 |
| D | HOH401 |
| D | HOH407 |
| D | HOH455 |
| D | HOH459 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue CL D 302 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO D 303 |
| Chain | Residue |
| D | TYR177 |
| D | GLU227 |
| D | VAL232 |
| D | HOH503 |
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 | |
