Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0017001 | biological_process | antibiotic catabolic process |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046677 | biological_process | response to antibiotic |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0008800 | molecular_function | beta-lactamase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0017001 | biological_process | antibiotic catabolic process |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0046677 | biological_process | response to antibiotic |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0008800 | molecular_function | beta-lactamase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0017001 | biological_process | antibiotic catabolic process |
| D | 0042597 | cellular_component | periplasmic space |
| 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 | 4 |
| Details | binding site for residue ZN A 301 |
| Chain | Residue |
| A | HIS78 |
| A | HIS80 |
| A | HIS140 |
| A | LMP303 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 302 |
| Chain | Residue |
| A | ASP82 |
| A | CYS159 |
| A | HIS201 |
| A | LMP303 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for residue LMP A 303 |
| Chain | Residue |
| A | TRP52 |
| A | HIS80 |
| A | ASP82 |
| A | HIS140 |
| A | LYS162 |
| A | LEU169 |
| A | GLY170 |
| A | TYR171 |
| A | HIS201 |
| A | ZN301 |
| A | ZN302 |
| A | ILE32 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 301 |
| Chain | Residue |
| B | HIS78 |
| B | HIS80 |
| B | HIS140 |
| B | LMP303 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 302 |
| Chain | Residue |
| B | ASP82 |
| B | CYS159 |
| B | HIS201 |
| B | LMP303 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | binding site for residue LMP B 303 |
| Chain | Residue |
| B | ILE32 |
| B | HIS80 |
| B | ASP82 |
| B | HIS140 |
| B | CYS159 |
| B | LYS162 |
| B | SER163 |
| B | ASN166 |
| B | TYR171 |
| B | HIS201 |
| B | ZN301 |
| B | ZN302 |
| B | HOH401 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 301 |
| Chain | Residue |
| C | HIS78 |
| C | HIS80 |
| C | HIS140 |
| C | LMP303 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 302 |
| Chain | Residue |
| C | ASP82 |
| C | CYS159 |
| C | HIS201 |
| C | LMP303 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | binding site for residue LMP C 303 |
| Chain | Residue |
| C | TRP29 |
| C | TRP52 |
| C | HIS80 |
| C | ASP82 |
| C | HIS140 |
| C | CYS159 |
| C | LYS162 |
| C | ASN166 |
| C | GLY170 |
| C | TYR171 |
| C | HIS201 |
| C | ZN301 |
| C | ZN302 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 301 |
| Chain | Residue |
| D | HIS78 |
| D | HIS80 |
| D | HIS140 |
| D | LMP303 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 302 |
| Chain | Residue |
| D | ASP82 |
| D | CYS159 |
| D | HIS201 |
| D | LMP303 |
| site_id | AD3 |
| Number of Residues | 15 |
| Details | binding site for residue LMP D 303 |
| Chain | Residue |
| D | TRP52 |
| D | HIS80 |
| D | GLU81 |
| D | ASP82 |
| D | HIS140 |
| D | CYS159 |
| D | VAL161 |
| D | LYS162 |
| D | SER163 |
| D | ASN166 |
| D | TYR171 |
| D | GLY200 |
| D | HIS201 |
| D | ZN301 |
| D | ZN302 |
Functional Information from PROSITE/UniProt
| site_id | PS00744 |
| Number of Residues | 13 |
| Details | BETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PnekILfGgCFVK |
| Chain | Residue | Details |
| A | PRO150-LYS162 | |
