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 1 |
| Chain | Residue |
| A | ZN2 |
| A | HIS99 |
| A | HIS101 |
| A | HIS162 |
| A | HOH250 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 2 |
| Chain | Residue |
| A | HOH250 |
| A | HOH251 |
| A | ZN1 |
| A | ASP103 |
| A | CYS181 |
| A | HIS223 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 3 |
| Chain | Residue |
| A | ASN55 |
| A | ASP69 |
| A | ASP103 |
| A | HOH255 |
| A | HOH263 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 1 |
| Chain | Residue |
| B | ZN2 |
| B | HIS99 |
| B | HIS101 |
| B | HIS162 |
| B | HOH250 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 2 |
| Chain | Residue |
| B | ZN1 |
| B | ASP103 |
| B | CYS181 |
| B | HIS223 |
| B | HOH250 |
| B | HOH251 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 3 |
| Chain | Residue |
| B | ASN55 |
| B | ASP69 |
| B | ASP103 |
| B | HOH255 |
| B | HOH264 |
Functional Information from PROSITE/UniProt
| site_id | PS00743 |
| Number of Residues | 20 |
| Details | BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IpNHwHGDciGGlgylqkk.G |
| Chain | Residue | Details |
| A | ILE96-GLY115 | |
| site_id | PS00744 |
| Number of Residues | 13 |
| Details | BETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PtenILfGgCMLK |
| Chain | Residue | Details |
| A | PRO172-LYS184 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | HIS99 | |
| A | HIS101 | |
| A | HIS162 | |
| B | HIS99 | |
| B | HIS101 | |
| B | HIS162 | |
| Chain | Residue | Details |
| A | ASP103 | |
| A | CYS181 | |
| A | HIS223 | |
| B | ASP103 | |
| B | CYS181 | |
| B | HIS223 | |
| Chain | Residue | Details |
| A | LYS184 | |
| B | LYS184 | |
| Chain | Residue | Details |
| A | ASN193 | |
| B | ASN193 | |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 15 |
| Chain | Residue | Details |
| A | HIS99 | metal ligand |
| A | HIS101 | metal ligand |
| A | ASP103 | metal ligand |
| A | HIS162 | metal ligand |
| A | CYS181 | metal ligand |
| A | LYS184 | electrostatic stabiliser, steric role |
| A | ASN193 | electrostatic stabiliser, hydrogen bond donor |
| A | HIS223 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 8 |
| Details | M-CSA 15 |
| Chain | Residue | Details |
| B | HIS99 | metal ligand |
| B | HIS101 | metal ligand |
| B | ASP103 | metal ligand |
| B | HIS162 | metal ligand |
| B | CYS181 | metal ligand |
| B | LYS184 | electrostatic stabiliser, steric role |
| B | ASN193 | electrostatic stabiliser, hydrogen bond donor |
| B | HIS223 | metal ligand |
