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 | 9 |
| Details | BINDING SITE FOR RESIDUE X8Z A 300 |
| Chain | Residue |
| A | TRP46 |
| A | ASP99 |
| A | HIS157 |
| A | LYS179 |
| A | ASN185 |
| A | HIS215 |
| A | ZN501 |
| A | ZN502 |
| A | HOH2061 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 400 |
| Chain | Residue |
| A | TYR35 |
| A | ARG84 |
| A | TYR86 |
| A | LYS170 |
| A | HOH2119 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 401 |
| Chain | Residue |
| A | VAL56 |
| A | LEU57 |
| A | GLU168 |
| A | ARG169 |
| A | HOH2108 |
| A | HOH2147 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 402 |
| Chain | Residue |
| A | TRP80 |
| A | ARG84 |
| A | GLU168 |
| A | ARG169 |
| A | HOH2045 |
| A | HOH2148 |
| A | HOH2149 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 501 |
| Chain | Residue |
| A | HIS95 |
| A | HIS97 |
| A | HIS157 |
| A | X8Z300 |
| A | ZN502 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 502 |
| Chain | Residue |
| A | ASP99 |
| A | CYS176 |
| A | HIS215 |
| A | X8Z300 |
| A | ZN501 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 501 |
| Chain | Residue |
| B | ASP99 |
| B | CYS176 |
| B | HIS215 |
| B | ZN502 |
| B | HOH2004 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 502 |
| Chain | Residue |
| B | HIS95 |
| B | HIS97 |
| B | HIS157 |
| B | CYS176 |
| B | ZN501 |
| B | HOH2004 |
Functional Information from PROSITE/UniProt
| site_id | PS00743 |
| Number of Residues | 20 |
| Details | BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IsSHfHSDstGGiewlnsr.S |
| Chain | Residue | Details |
| A | ILE92-SER111 | |
| site_id | PS00744 |
| Number of Residues | 13 |
| Details | BETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PerkILfGgCFIK |
| Chain | Residue | Details |
| A | PRO167-LYS179 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | HIS95 | |
| B | ASP99 | |
| B | HIS157 | |
| B | CYS176 | |
| B | LYS179 | |
| B | HIS215 | |
| A | HIS97 | |
| A | ASP99 | |
| A | HIS157 | |
| A | CYS176 | |
| A | LYS179 | |
| A | HIS215 | |
| B | HIS95 | |
| B | HIS97 | |
| Chain | Residue | Details |
| A | ASN185 | |
| B | ASN185 | |
