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 |
| 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 |
| C | 0071555 | biological_process | cell wall organization |
| 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 |
| D | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue TVZ A 301 |
| Chain | Residue |
| A | TYR117 |
| A | THR209 |
| A | ARG250 |
| A | HOH547 |
| A | HOH558 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| B | MET138 |
| A | HIS38 |
| A | GLU256 |
| A | HOH447 |
| B | ARG134 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | ASN152 |
| A | HOH460 |
| D | TRP95 |
| D | ARG107 |
| D | ASP108 |
| D | HOH473 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue TVZ B 301 |
| Chain | Residue |
| B | TYR117 |
| B | THR209 |
| B | TYR211 |
| B | ARG250 |
| B | HOH413 |
| B | HOH420 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 302 |
| Chain | Residue |
| B | ILE130 |
| B | GLY131 |
| B | GLU132 |
| B | ALA133 |
| B | ARG134 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue TVZ C 301 |
| Chain | Residue |
| C | ILE102 |
| C | TYR117 |
| C | TYR211 |
| C | ARG250 |
| C | HOH401 |
| C | HOH405 |
| C | HOH432 |
| C | HOH623 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue CL C 302 |
| Chain | Residue |
| B | ARG206 |
| C | ARG206 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue EDO C 303 |
| Chain | Residue |
| B | GLY151 |
| B | ASP159 |
| B | HOH457 |
| B | HOH461 |
| C | LYS94 |
| C | TRP95 |
| C | ASP108 |
| C | HOH449 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 304 |
| Chain | Residue |
| C | LEU81 |
| C | SER184 |
| C | ARG186 |
| C | SER187 |
| C | HOH416 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue EDO C 305 |
| Chain | Residue |
| B | HIS90 |
| B | HOH424 |
| C | TYR177 |
| C | GLU227 |
| C | VAL232 |
| C | HOH409 |
| C | HOH478 |
| site_id | AD2 |
| Number of Residues | 9 |
| Details | binding site for residue TVZ D 301 |
| Chain | Residue |
| D | TYR117 |
| D | THR209 |
| D | TYR211 |
| D | LEU247 |
| D | ARG250 |
| D | HOH409 |
| D | HOH450 |
| D | HOH479 |
| D | HOH480 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue CL D 302 |
| Chain | Residue |
| A | ARG206 |
| D | ARG206 |
| D | HOH580 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue EDO D 303 |
| Chain | Residue |
| A | ASP229 |
| D | HOH550 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 304 |
| Chain | Residue |
| D | ASN48 |
| D | LYS51 |
| D | HOH414 |
| D | HOH417 |
| D | HOH503 |
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 | |
