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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue PG4 A 301 |
| Chain | Residue |
| A | ALA40 |
| A | HOH556 |
| B | ASP177 |
| B | PRO178 |
| B | ARG179 |
| B | HOH582 |
| A | GLN89 |
| A | ARG94 |
| A | SER142 |
| A | PHE143 |
| A | GLY144 |
| A | HOH401 |
| A | HOH527 |
| A | HOH545 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue PEG A 302 |
| Chain | Residue |
| A | ASP198 |
| A | LEU200 |
| A | ARG205 |
| A | HOH528 |
| B | GLY229 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue FMT A 303 |
| Chain | Residue |
| A | SER131 |
| A | LYS235 |
| A | THR236 |
| A | GLY237 |
| A | THR238 |
| A | EDO304 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | CYS70 |
| A | SER71 |
| A | ASN133 |
| A | GLY237 |
| A | THR238 |
| A | FMT303 |
| A | HOH405 |
| A | HOH464 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 305 |
| Chain | Residue |
| A | GLU159 |
| A | THR160 |
| A | HOH603 |
| B | ARG205 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 306 |
| Chain | Residue |
| A | ARG87 |
| B | GLY229 |
| B | TRP230 |
| B | LEU253 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 301 |
| Chain | Residue |
| B | SER131 |
| B | LYS235 |
| B | THR236 |
| B | GLY237 |
| B | THR238 |
| B | FMT302 |
| B | HOH409 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue FMT B 302 |
| Chain | Residue |
| B | CYS70 |
| B | SER71 |
| B | GLY237 |
| B | THR238 |
| B | EDO301 |
| B | HOH403 |
| B | HOH404 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 303 |
| Chain | Residue |
| B | ARG185 |
| B | GLN189 |
Functional Information from PROSITE/UniProt
| site_id | PS00146 |
| Number of Residues | 16 |
| Details | BETA_LACTAMASE_A Beta-lactamase class-A active site. FpMCSTfKvlaAGLVL |
| Chain | Residue | Details |
| A | PHE67-LEU82 | |
