Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0017001 | biological_process | antibiotic catabolic process |
| A | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| A | 0046677 | biological_process | response to antibiotic |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
| B | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| B | 0046677 | biological_process | response to antibiotic |
| C | 0008800 | molecular_function | beta-lactamase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0017001 | biological_process | antibiotic catabolic process |
| C | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| C | 0046677 | biological_process | response to antibiotic |
| D | 0008800 | molecular_function | beta-lactamase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0017001 | biological_process | antibiotic catabolic process |
| D | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| D | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 301 |
| Chain | Residue |
| A | SER43 |
| A | ASN45 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 302 |
| Chain | Residue |
| A | ARG103 |
| B | GLN208 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue PGE A 303 |
| Chain | Residue |
| A | ARG278 |
| A | ASP211 |
| A | ARG215 |
| A | ALA216 |
| A | LEU218 |
| A | ASP220 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue CIT A 304 |
| Chain | Residue |
| A | SER62 |
| A | TYR97 |
| A | SER123 |
| A | THR209 |
| A | THR228 |
| A | GLY229 |
| A | SER230 |
| A | ARG236 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue MRD A 305 |
| Chain | Residue |
| A | GLN121 |
| A | GLN208 |
| A | HOH497 |
| B | TYR104 |
| B | GLU114 |
| B | SER118 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue PGE B 301 |
| Chain | Residue |
| B | ASP211 |
| B | ARG215 |
| B | ALA216 |
| B | LEU218 |
| B | PRO219 |
| B | ASP220 |
| B | TRP222 |
| B | THR224 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | binding site for residue CIT B 302 |
| Chain | Residue |
| B | SER62 |
| B | TYR97 |
| B | LEU122 |
| B | SER123 |
| B | ASN125 |
| B | THR209 |
| B | LYS227 |
| B | THR228 |
| B | GLY229 |
| B | SER230 |
| B | HOH401 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue CIT C 301 |
| Chain | Residue |
| C | SER62 |
| C | TYR97 |
| C | SER123 |
| C | THR209 |
| C | THR228 |
| C | GLY229 |
| C | SER230 |
| C | HOH402 |
| C | HOH416 |
| C | HOH526 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue CL D 301 |
| Chain | Residue |
| D | GLU96 |
| D | TYR97 |
| D | ALA98 |
| D | PRO99 |
| D | LYS102 |
| D | HOH612 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue CL D 302 |
| Chain | Residue |
| D | CYS61 |
| D | SER62 |
| D | THR63 |
| D | CYS231 |
| D | ASN237 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue IPA D 303 |
| Chain | Residue |
| D | LYS86 |
| D | HIS88 |
| D | HOH402 |
| D | HOH438 |
| D | HOH517 |
| D | HOH525 |
Functional Information from PROSITE/UniProt
| site_id | PS00146 |
| Number of Residues | 16 |
| Details | BETA_LACTAMASE_A Beta-lactamase class-A active site. FaMCSTfKlplAALVL |
| Chain | Residue | Details |
| A | PHE58-LEU73 |
