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 | 6 |
| Details | binding site for residue AUV A 301 |
| Chain | Residue |
| A | ARG250 |
| A | HOH409 |
| A | HOH503 |
| A | HOH504 |
| A | HOH569 |
| A | HOH601 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 302 |
| Chain | Residue |
| C | HOH621 |
| A | ARG206 |
| A | HOH664 |
| C | ARG206 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | HIS90 |
| A | HOH426 |
| A | HOH442 |
| C | TYR177 |
| C | GLU227 |
| C | VAL232 |
| C | HOH530 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | GLN124 |
| A | ASP154 |
| A | HOH498 |
| B | ASN152 |
| B | ASP159 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue AUV B 301 |
| Chain | Residue |
| B | TYR117 |
| B | ARG250 |
| B | HOH402 |
| B | HOH403 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 302 |
| Chain | Residue |
| B | ARG206 |
| B | HOH640 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 303 |
| Chain | Residue |
| B | LEU81 |
| B | SER184 |
| B | ARG186 |
| B | SER187 |
| B | HOH477 |
| B | HOH504 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 304 |
| Chain | Residue |
| B | LYS116 |
| B | HOH420 |
| B | HOH515 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 305 |
| Chain | Residue |
| B | TRP25 |
| B | SER171 |
| B | ARG174 |
| B | HOH432 |
| B | HOH442 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 306 |
| Chain | Residue |
| B | LYS94 |
| B | TRP95 |
| B | ASP96 |
| B | VAL122 |
| B | HOH465 |
| site_id | AD2 |
| Number of Residues | 8 |
| Details | binding site for residue AUV C 301 |
| Chain | Residue |
| C | ILE102 |
| C | TYR117 |
| C | THR209 |
| C | TYR211 |
| C | ARG250 |
| C | HOH401 |
| C | HOH421 |
| C | HOH428 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 302 |
| Chain | Residue |
| C | VAL85 |
| C | GLN91 |
| C | PHE93 |
| C | GLN129 |
| C | HOH467 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO C 303 |
| Chain | Residue |
| C | THR167 |
| C | SER171 |
| C | ARG174 |
| site_id | AD5 |
| Number of Residues | 2 |
| Details | binding site for residue EDO C 304 |
| Chain | Residue |
| C | ARG100 |
| C | ASP101 |
| site_id | AD6 |
| Number of Residues | 8 |
| Details | binding site for residue AUV D 301 |
| Chain | Residue |
| D | ILE102 |
| D | TYR117 |
| D | THR209 |
| D | TYR211 |
| D | ARG250 |
| D | HOH426 |
| D | HOH563 |
| D | HOH610 |
| site_id | AD7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO D 302 |
| Chain | Residue |
| D | TYR177 |
| D | GLU227 |
| D | HOH506 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue EDO D 303 |
| Chain | Residue |
| D | LEU81 |
| D | SER184 |
| D | ARG186 |
| D | SER187 |
| D | HOH484 |
| D | HOH592 |
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 | |
