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 | HIS77 |
| A | HIS79 |
| A | HIS139 |
| A | ZN302 |
| A | HOH478 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue ZN A 302 |
| Chain | Residue |
| A | HOH426 |
| A | HOH478 |
| A | ASP81 |
| A | CYS158 |
| A | HIS197 |
| A | ZN301 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | GLU14 |
| A | GLY15 |
| A | LEU39 |
| A | GLU150 |
| A | ARG151 |
| A | HOH438 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue ACT A 304 |
| Chain | Residue |
| A | SER99 |
| A | PHE118 |
| A | SER119 |
| A | GLY120 |
| A | TYR134 |
| A | VAL144 |
| A | HOH413 |
| A | HOH495 |
| A | HOH498 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 301 |
| Chain | Residue |
| B | HIS77 |
| B | HIS79 |
| B | HIS139 |
| B | ZN302 |
| B | HOH476 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 302 |
| Chain | Residue |
| B | ASP81 |
| B | CYS158 |
| B | HIS197 |
| B | ZN301 |
| B | HOH476 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 303 |
| Chain | Residue |
| B | GLU14 |
| B | VAL38 |
| B | LEU39 |
| B | GLU150 |
| B | ARG151 |
| B | HOH444 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue ZN C 301 |
| Chain | Residue |
| C | ASP81 |
| C | CYS158 |
| C | HIS197 |
| C | ZN302 |
| C | HOH515 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue ZN C 302 |
| Chain | Residue |
| C | HIS77 |
| C | HIS79 |
| C | HIS139 |
| C | ZN301 |
| C | HOH515 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue ZN D 301 |
| Chain | Residue |
| D | HIS77 |
| D | HIS79 |
| D | HIS139 |
| D | ZN302 |
| D | HOH429 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue ZN D 302 |
| Chain | Residue |
| D | ASP81 |
| D | CYS158 |
| D | HIS197 |
| D | ZN301 |
| D | HOH429 |
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 | ILE74-SER93 | |
| site_id | PS00744 |
| Number of Residues | 13 |
| Details | BETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PerkILfGgCFIK |
| Chain | Residue | Details |
| A | PRO149-LYS161 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | HIS77 | |
| B | ASP81 | |
| B | HIS139 | |
| B | CYS158 | |
| B | LYS161 | |
| B | HIS197 | |
| C | HIS77 | |
| C | HIS79 | |
| C | ASP81 | |
| C | HIS139 | |
| C | CYS158 | |
| A | HIS79 | |
| C | LYS161 | |
| C | HIS197 | |
| D | HIS77 | |
| D | HIS79 | |
| D | ASP81 | |
| D | HIS139 | |
| D | CYS158 | |
| D | LYS161 | |
| D | HIS197 | |
| A | ASP81 | |
| A | HIS139 | |
| A | CYS158 | |
| A | LYS161 | |
| A | HIS197 | |
| B | HIS77 | |
| B | HIS79 | |
| Chain | Residue | Details |
| A | ASN167 | |
| B | ASN167 | |
| C | ASN167 | |
| D | ASN167 | |
