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 | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 228 |
| Chain | Residue |
| A | HIS86 |
| A | HIS88 |
| A | HIS149 |
| A | HOH400 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 229 |
| Chain | Residue |
| A | ASP90 |
| A | CYS168 |
| A | HIS210 |
| A | HOH313 |
| A | HOH400 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 230 |
| Chain | Residue |
| A | SER172 |
| A | THR173 |
| A | SER174 |
| A | GLY211 |
| A | GLU212 |
| A | HOH270 |
| A | HOH295 |
| A | HOH301 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 228 |
| Chain | Residue |
| B | HIS86 |
| B | HIS88 |
| B | HIS149 |
| B | HOH302 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 229 |
| Chain | Residue |
| B | ASP90 |
| B | CYS168 |
| B | HIS210 |
| B | HOH292 |
| B | HOH302 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 230 |
| Chain | Residue |
| B | SER172 |
| B | THR173 |
| B | SER174 |
| B | GLY211 |
| B | GLU212 |
| B | HOH258 |
| site_id | ASA |
| Number of Residues | 1 |
| Details | STRAINED BURIED RESIDUE, CLOSE TO ACTIVE SITE IN MOLECULE A. |
| site_id | ASB |
| Number of Residues | 1 |
| Details | STRAINED BURIED RESIDUE, CLOSE TO ACTIVE SITE IN MOLECULE B . |
| site_id | ZNA |
| Number of Residues | 6 |
| Details | ZINC BINDING SITES AND ACTIVE SITE FOR MOLECULE A. |
| Chain | Residue |
| A | HIS86 |
| A | HIS88 |
| A | ASP90 |
| A | HIS149 |
| A | CYS168 |
| A | HIS210 |
| site_id | ZNB |
| Number of Residues | 6 |
| Details | ZINC BINDING SITES AND ACTIVE SITE FOR MOLECULE B. |
| Chain | Residue |
| B | HIS149 |
| B | CYS168 |
| B | HIS210 |
| B | HIS86 |
| B | HIS88 |
| B | ASP90 |
Functional Information from PROSITE/UniProt
| site_id | PS00743 |
| Number of Residues | 20 |
| Details | BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IiTHaHADriGGiktlker.G |
| Chain | Residue | Details |
| A | ILE83-GLY102 | |
| site_id | PS00744 |
| Number of Residues | 13 |
| Details | BETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PqynILvGgCLVK |
| Chain | Residue | Details |
| A | PRO159-LYS171 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | HIS86 | |
| A | HIS88 | |
| A | HIS149 | |
| B | HIS86 | |
| B | HIS88 | |
| B | HIS149 | |
| Chain | Residue | Details |
| A | ASP90 | |
| A | CYS168 | |
| A | HIS210 | |
| B | ASP90 | |
| B | CYS168 | |
| B | HIS210 | |
| Chain | Residue | Details |
| A | LYS171 | |
| B | LYS171 | |
| Chain | Residue | Details |
| A | ASN180 | |
| B | ASN180 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| A | ASP90 | |
| A | ASN180 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| B | ASP90 | |
| B | ASN180 | |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| A | ASP90 | |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| B | ASP90 | |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 16 |
| Chain | Residue | Details |
| A | HIS86 | metal ligand |
| A | HIS88 | metal ligand |
| A | ASP90 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | HIS149 | metal ligand |
| A | ASN180 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 16 |
| Chain | Residue | Details |
| B | HIS86 | metal ligand |
| B | HIS88 | metal ligand |
| B | ASP90 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | HIS149 | metal ligand |
| B | ASN180 | electrostatic stabiliser, hydrogen bond donor |
