Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005886 | cellular_component | plasma membrane |
| 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 | 0071555 | biological_process | cell wall organization |
| B | 0005886 | cellular_component | plasma membrane |
| 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 | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue FLC A 301 |
| Chain | Residue |
| A | GLN100 |
| A | HOH413 |
| A | HOH416 |
| A | HOH477 |
| A | HOH564 |
| A | SER101 |
| A | TRP136 |
| A | SER149 |
| A | VAL151 |
| A | LYS239 |
| A | THR240 |
| A | GLY241 |
| A | SER242 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue FLC A 302 |
| Chain | Residue |
| A | HIS168 |
| A | LYS171 |
| A | ALA172 |
| A | HIS285 |
| A | HOH408 |
| A | HOH514 |
| A | HOH550 |
| A | HOH750 |
| A | HOH769 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | ARG147 |
| A | VAL227 |
| A | GLN228 |
| A | HOH492 |
| A | HOH558 |
| B | LYS217 |
| B | HOH492 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | LYS217 |
| A | HOH476 |
| A | HOH498 |
| A | HOH501 |
| A | HOH510 |
| B | ARG147 |
| B | GLN228 |
| B | GLU230 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue FLC B 301 |
| Chain | Residue |
| B | GLN100 |
| B | SER101 |
| B | TRP136 |
| B | SER149 |
| B | VAL151 |
| B | LYS239 |
| B | THR240 |
| B | GLY241 |
| B | SER242 |
| B | HOH419 |
| B | HOH459 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue PEG B 302 |
| Chain | Residue |
| B | LYS283 |
| B | TYR284 |
| B | HIS285 |
| B | HOH458 |
| B | HOH583 |
Functional Information from PROSITE/UniProt
| site_id | PS00337 |
| Number of Residues | 11 |
| Details | BETA_LACTAMASE_D Beta-lactamase class-D active site. PqSTFKVAnAL |
| Chain | Residue | Details |
| A | PRO99-LEU109 | |