Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0017001 | biological_process | antibiotic catabolic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 251 |
| Chain | Residue |
| A | HIS82 |
| A | HIS84 |
| A | HIS145 |
| A | 061250 |
| A | ZN252 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 252 |
| Chain | Residue |
| A | 061250 |
| A | ZN251 |
| A | ASP86 |
| A | HIS145 |
| A | CYS164 |
| A | HIS206 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 251 |
| Chain | Residue |
| B | HIS82 |
| B | HIS84 |
| B | HIS145 |
| B | ZN252 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 252 |
| Chain | Residue |
| B | ASP86 |
| B | HIS145 |
| B | CYS164 |
| B | HIS206 |
| B | ZN251 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 061 A 250 |
| Chain | Residue |
| A | ILE29 |
| A | TRP32 |
| A | VAL35 |
| A | HIS145 |
| A | CYS164 |
| A | ASP168 |
| A | GLY175 |
| A | ASN176 |
| A | HIS206 |
| A | GLY207 |
| A | ASN208 |
| A | ZN251 |
| A | ZN252 |
| A | HOH282 |
| A | HOH315 |
Functional Information from PROSITE/UniProt
| site_id | PS00743 |
| Number of Residues | 20 |
| Details | BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IpNHwHGDciGGlgylqrk.G |
| Chain | Residue | Details |
| A | ILE79-GLY98 | |
| site_id | PS00744 |
| Number of Residues | 13 |
| Details | BETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PtenILfGgCMLK |
| Chain | Residue | Details |
| A | PRO155-LYS167 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | HIS82 | |
| A | HIS84 | |
| A | HIS145 | |
| B | HIS82 | |
| B | HIS84 | |
| B | HIS145 | |
| Chain | Residue | Details |
| A | ASP86 | |
| A | CYS164 | |
| A | HIS206 | |
| B | ASP86 | |
| B | CYS164 | |
| B | HIS206 | |
| Chain | Residue | Details |
| A | LYS167 | |
| B | LYS167 | |
| Chain | Residue | Details |
| A | ASN176 | |
| B | ASN176 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| A | ASP86 | |
| A | ASN176 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| B | ASP86 | |
| B | ASN176 | |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| A | ASP86 | |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| B | ASP86 | |
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 15 |
| Chain | Residue | Details |
| A | HIS82 | metal ligand |
| A | HIS84 | metal ligand |
| A | ASP86 | metal ligand |
| A | HIS145 | metal ligand |
| A | CYS164 | metal ligand |
| A | LYS167 | electrostatic stabiliser, steric role |
| A | ASN176 | electrostatic stabiliser, hydrogen bond donor |
| A | HIS206 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 8 |
| Details | M-CSA 15 |
| Chain | Residue | Details |
| B | HIS82 | metal ligand |
| B | HIS84 | metal ligand |
| B | ASP86 | metal ligand |
| B | HIS145 | metal ligand |
| B | CYS164 | metal ligand |
| B | LYS167 | electrostatic stabiliser, steric role |
| B | ASN176 | electrostatic stabiliser, hydrogen bond donor |
| B | HIS206 | metal ligand |
