Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008658 | molecular_function | penicillin binding |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0017001 | biological_process | antibiotic catabolic process |
| B | 0008658 | molecular_function | penicillin binding |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
| C | 0008658 | molecular_function | penicillin binding |
| C | 0008800 | molecular_function | beta-lactamase activity |
| C | 0017001 | biological_process | antibiotic catabolic process |
| D | 0008658 | molecular_function | penicillin binding |
| D | 0008800 | molecular_function | beta-lactamase activity |
| D | 0017001 | biological_process | antibiotic catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 301 |
| Chain | Residue |
| A | GLN100 |
| A | SER101 |
| A | LEU189 |
| A | GLY241 |
| A | THR242 |
| A | HOH402 |
| A | HOH414 |
| A | HOH416 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue PEG A 302 |
| Chain | Residue |
| A | ALA116 |
| A | ASP160 |
| A | ARG165 |
| A | HOH515 |
| A | VAL114 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue MLI B 301 |
| Chain | Residue |
| B | SER101 |
| B | LYS104 |
| B | GLU148 |
| B | SER149 |
| B | LYS239 |
| B | THR240 |
| B | GLY241 |
| B | THR242 |
| B | HOH476 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue MLI B 302 |
| Chain | Residue |
| B | ALA208 |
| B | LYS223 |
| B | TYR237 |
| B | SER259 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue PEG B 303 |
| Chain | Residue |
| B | VAL114 |
| B | ALA116 |
| B | ASP160 |
| B | ARG165 |
| B | HOH569 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue MLI D 301 |
| Chain | Residue |
| D | SER101 |
| D | LYS104 |
| D | GLU148 |
| D | SER149 |
| D | LYS239 |
| D | THR240 |
| D | GLY241 |
| D | HOH421 |
| D | HOH427 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 302 |
| Chain | Residue |
| C | ARG147 |
| C | ILE227 |
| C | GLN228 |
| D | ARG224 |
| D | HOH412 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue EDO D 303 |
| Chain | Residue |
| D | MET146 |
| D | ARG147 |
| D | GLN228 |
| D | LYS239 |
| D | THR240 |
| D | HOH456 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO D 304 |
| Chain | Residue |
| D | LYS223 |
| D | LYS254 |
| D | SER259 |
Functional Information from PROSITE/UniProt
| site_id | PS00337 |
| Number of Residues | 11 |
| Details | BETA_LACTAMASE_D Beta-lactamase class-D active site. PqSTFKVVnAL |
| Chain | Residue | Details |
| B | PRO99-LEU109 | |
| A | PRO99-LEU109 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| B | SER101 | |
| D | SER101 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| B | LYS239 | |
| D | LYS239 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-carboxylysine => ECO:0000250 |
| Chain | Residue | Details |
| B | LYS104 | |
| D | LYS104 | |
