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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 317 |
| Chain | Residue |
| A | HIS116 |
| A | HIS118 |
| A | HIS196 |
| A | CSD221 |
| A | HOH594 |
| A | HOH710 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 317 |
| Chain | Residue |
| B | HOH664 |
| B | HOH728 |
| B | HIS116 |
| B | HIS118 |
| B | HIS196 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE AZI A 401 |
| Chain | Residue |
| A | HIS196 |
| A | CSD221 |
| A | LYS224 |
| A | GLY232 |
| A | TYR233 |
| B | TYR67 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE AZI B 402 |
| Chain | Residue |
| A | TYR67 |
| B | HIS196 |
| B | CSO221 |
| B | LYS224 |
| B | TYR233 |
| B | HIS263 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE AZI A 403 |
| Chain | Residue |
| A | SER84 |
| A | THR115 |
| A | HIS116 |
| A | GLY220 |
| A | CSD221 |
| A | HOH624 |
| A | HOH704 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 601 |
| Chain | Residue |
| B | ARG150 |
| B | HIS164 |
| B | HOH653 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 501 |
| Chain | Residue |
| A | LEU249 |
| A | LYS250 |
| A | PHE252 |
| A | ALA256 |
| A | PRO297 |
| A | VAL300 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 502 |
| Chain | Residue |
| A | GLU265 |
| A | TRP266 |
| A | GLU313 |
| A | ARG315 |
| A | HOH722 |
Functional Information from PROSITE/UniProt
| site_id | PS00744 |
| Number of Residues | 13 |
| Details | BETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PkkkLLfGgCMIK |
| Chain | Residue | Details |
| A | PRO206-LYS224 | |
| B | PRO206-LYS224 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qh5 |
| Chain | Residue | Details |
| A | ASP120 | |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qh5 |
| Chain | Residue | Details |
| B | ASP120 | |
