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 | 2 |
| Details | binding site for residue CL A 301 |
| Chain | Residue |
| A | ARG206 |
| B | ARG206 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 302 |
| Chain | Residue |
| A | LYS73 |
| A | TRP157 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue MER A 303 |
| Chain | Residue |
| A | LEU158 |
| A | LYS208 |
| A | THR209 |
| A | GLY210 |
| A | TYR211 |
| A | ARG250 |
| A | ALA69 |
| A | SER70 |
| A | TRP105 |
| A | SER118 |
| A | VAL120 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 301 |
| Chain | Residue |
| B | LYS73 |
| B | TRP157 |
| B | HOH462 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue CL C 301 |
| Chain | Residue |
| C | ARG206 |
| D | ARG206 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue CL C 302 |
| Chain | Residue |
| C | LYS73 |
| C | TRP157 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue GOL C 304 |
| Chain | Residue |
| C | LYS94 |
| C | TRP95 |
| C | ASP96 |
| C | PRO121 |
| C | VAL122 |
| C | HOH421 |
| C | HOH427 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue CL D 301 |
| Chain | Residue |
| D | LYS73 |
| D | VAL120 |
| D | TRP157 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue GOL D 303 |
| Chain | Residue |
| D | LYS94 |
| D | TRP95 |
| D | ASP96 |
| D | ARG100 |
| D | HOH409 |
| site_id | AD1 |
| Number of Residues | 14 |
| Details | binding site for Di-peptide MER B 302 and SER B 70 |
| Chain | Residue |
| B | PRO68 |
| B | ALA69 |
| B | THR71 |
| B | PHE72 |
| B | LYS73 |
| B | TRP105 |
| B | SER118 |
| B | VAL120 |
| B | LYS208 |
| B | THR209 |
| B | GLY210 |
| B | TYR211 |
| B | ARG250 |
| B | HOH455 |
| site_id | AD2 |
| Number of Residues | 13 |
| Details | binding site for Di-peptide MER C 303 and SER C 70 |
| Chain | Residue |
| C | PRO68 |
| C | ALA69 |
| C | THR71 |
| C | PHE72 |
| C | LYS73 |
| C | SER118 |
| C | VAL120 |
| C | LEU158 |
| C | LYS208 |
| C | THR209 |
| C | GLY210 |
| C | TYR211 |
| C | ARG250 |
| site_id | AD3 |
| Number of Residues | 14 |
| Details | binding site for Di-peptide MER D 302 and SER D 70 |
| Chain | Residue |
| D | PRO68 |
| D | ALA69 |
| D | THR71 |
| D | PHE72 |
| D | LYS73 |
| D | TRP105 |
| D | SER118 |
| D | VAL120 |
| D | LEU158 |
| D | LYS208 |
| D | THR209 |
| D | GLY210 |
| D | TYR211 |
| D | ARG250 |
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 | |
