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 |
| 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 |
| 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 |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue U3M A 301 |
| Chain | Residue |
| A | SER70 |
| A | ARG250 |
| A | HOH403 |
| A | HOH410 |
| A | HOH412 |
| A | HOH468 |
| A | HOH617 |
| A | ILE102 |
| A | THR104 |
| A | TYR117 |
| A | VAL120 |
| A | LEU158 |
| A | THR209 |
| A | GLY210 |
| A | TYR211 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| A | LYS94 |
| A | TRP95 |
| A | ASP96 |
| A | VAL122 |
| A | HOH437 |
| A | HOH562 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | ASN200 |
| A | GLY201 |
| A | ASP202 |
| A | TYR203 |
| A | GLU227 |
| A | ASP229 |
| A | HOH401 |
| A | HOH578 |
| C | LYS116 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | GLN64 |
| A | ALA65 |
| A | PHE66 |
| A | PRO217 |
| A | HOH469 |
| A | HOH513 |
| A | HOH523 |
| A | HOH721 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | binding site for residue U3M B 301 |
| Chain | Residue |
| B | ILE102 |
| B | THR104 |
| B | TRP105 |
| B | TYR117 |
| B | THR209 |
| B | GLY210 |
| B | TYR211 |
| B | THR213 |
| B | ARG250 |
| B | HOH401 |
| B | HOH403 |
| B | HOH406 |
| B | HOH409 |
| B | HOH701 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 302 |
| Chain | Residue |
| B | ARG206 |
| B | HOH654 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue CL C 301 |
| Chain | Residue |
| A | ARG206 |
| A | HOH667 |
| C | ARG206 |
| C | HOH628 |
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 | |
