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 |
| A | 0071555 | biological_process | cell wall organization |
| 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 |
| B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue CD A 301 |
| Chain | Residue |
| A | GLU37 |
| A | HIS38 |
| A | GLU125 |
| A | GLU256 |
| A | CD304 |
| A | HOH547 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 302 |
| Chain | Residue |
| A | ARG206 |
| B | ARG206 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue CD A 303 |
| Chain | Residue |
| A | HOH555 |
| A | HOH586 |
| B | ASP143 |
| B | HOH502 |
| A | ASP143 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue CD A 304 |
| Chain | Residue |
| A | HIS34 |
| A | GLU37 |
| A | GLU256 |
| A | CD301 |
| A | HOH463 |
| A | HOH547 |
| A | HOH595 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | binding site for residue 5VW A 305 |
| Chain | Residue |
| A | ALA69 |
| A | SER70 |
| A | ASP101 |
| A | ILE102 |
| A | SER118 |
| A | VAL120 |
| A | LYS208 |
| A | THR209 |
| A | GLY210 |
| A | TYR211 |
| A | ARG250 |
| A | HOH479 |
| A | HOH499 |
| A | HOH538 |
| A | HOH541 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue CO A 306 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue CO B 301 |
| Chain | Residue |
| B | HIS34 |
| B | GLU37 |
| B | GLU256 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue CO B 302 |
| Chain | Residue |
| A | HIS140 |
| A | GLU147 |
| A | HOH453 |
| A | HOH480 |
| B | GLU147 |
| B | CO305 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | binding site for residue CO B 303 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue CO B 304 |
| Chain | Residue |
| A | HIS178 |
| B | HIS90 |
| B | HOH572 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue CO B 305 |
| Chain | Residue |
| A | GLU147 |
| A | HOH453 |
| A | HOH480 |
| B | HIS140 |
| B | GLU147 |
| B | CO302 |
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 | |
