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 | 5 |
| Details | binding site for residue ZN A 301 |
| Chain | Residue |
| A | HIS78 |
| A | HIS80 |
| A | HIS140 |
| A | ZN302 |
| A | HOH477 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 302 |
| Chain | Residue |
| A | HOH477 |
| A | ASP82 |
| A | CYS159 |
| A | HIS201 |
| A | ZN301 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 301 |
| Chain | Residue |
| B | HIS78 |
| B | HIS80 |
| B | HIS140 |
| B | ZN302 |
| B | HOH501 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 302 |
| Chain | Residue |
| B | ASP82 |
| B | CYS159 |
| B | HIS201 |
| B | ZN301 |
| B | HOH501 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 303 |
| Chain | Residue |
| B | LEU106 |
| B | THR141 |
| B | GLU142 |
| B | ASP174 |
| B | HOH463 |
| B | HOH492 |
| D | LYS211 |
| D | GLN214 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 304 |
| Chain | Residue |
| A | LYS153 |
| B | ALA138 |
| B | GLU142 |
| B | ASN176 |
| B | GLU179 |
| B | HOH476 |
| D | HIS212 |
| D | HOH427 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue ZN C 301 |
| Chain | Residue |
| C | HIS78 |
| C | HIS80 |
| C | HIS140 |
| C | ZN302 |
| C | HOH493 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue ZN C 302 |
| Chain | Residue |
| C | ASP82 |
| C | CYS159 |
| C | HIS201 |
| C | ZN301 |
| C | HOH493 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue ZN D 301 |
| Chain | Residue |
| D | HIS78 |
| D | HIS80 |
| D | HIS140 |
| D | ZN302 |
| D | HOH486 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue ZN D 302 |
| Chain | Residue |
| D | ASP82 |
| D | CYS159 |
| D | HIS201 |
| D | ZN301 |
| D | HOH486 |
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 | |
