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 | 9BZ303 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 302 |
| Chain | Residue |
| A | 9BZ303 |
| A | ASP81 |
| A | CYS158 |
| A | HIS197 |
| A | ZN301 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue 9BZ A 303 |
| Chain | Residue |
| A | TRP28 |
| A | HIS79 |
| A | ASP81 |
| A | HIS139 |
| A | LYS161 |
| A | GLY166 |
| A | ASN167 |
| A | HIS197 |
| A | ZN301 |
| A | ZN302 |
| A | EDO304 |
| A | HOH402 |
| D | GLU199 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | 9BZ303 |
| A | HOH456 |
| 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 | 9BZ303 |
| 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 | 9BZ303 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | binding site for residue 9BZ B 303 |
| Chain | Residue |
| B | VAL25 |
| B | TRP28 |
| B | HIS79 |
| B | ASP81 |
| B | HIS139 |
| B | LYS161 |
| B | GLY166 |
| B | ASN167 |
| B | HIS197 |
| B | ZN301 |
| B | ZN302 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 301 |
| Chain | Residue |
| C | HIS77 |
| C | HIS79 |
| C | HIS139 |
| C | 9BZ304 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 302 |
| Chain | Residue |
| C | ASP81 |
| C | CYS158 |
| C | HIS197 |
| C | 9BZ304 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue DMS C 303 |
| Chain | Residue |
| C | SER119 |
| C | GLY120 |
| C | TYR134 |
| C | VAL144 |
| C | HOH420 |
| site_id | AD2 |
| Number of Residues | 11 |
| Details | binding site for residue 9BZ C 304 |
| Chain | Residue |
| C | TRP28 |
| C | HIS79 |
| C | ASP81 |
| C | HIS139 |
| C | LYS161 |
| C | ASN167 |
| C | HIS197 |
| C | ZN301 |
| C | ZN302 |
| C | HOH404 |
| C | HOH407 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 301 |
| Chain | Residue |
| D | HIS77 |
| D | HIS79 |
| D | HIS139 |
| D | ZN302 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 302 |
| Chain | Residue |
| D | ASP81 |
| D | CYS158 |
| D | HIS197 |
| D | ZN301 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue 9BZ D 303 |
| Chain | Residue |
| D | ARG92 |
| D | LYS181 |
| D | VAL214 |
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
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P25910","evidenceCode":"ECO:0000250"}]} |