4C09
Crystal structure of the metallo-beta-lactamase BCII
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 300 |
| Chain | Residue |
| A | LYS95 |
| A | GLU130 |
| A | ARG131 |
| A | HOH2077 |
| A | HOH2086 |
| A | HOH2282 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 301 |
| Chain | Residue |
| A | ASP182 |
| A | HOH2196 |
| A | HOH2224 |
| A | ALA117 |
| A | ASN148 |
| A | THR180 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 303 |
| Chain | Residue |
| A | LYS103 |
| A | LYS169 |
| A | GLN190 |
| A | HOH2201 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 350 |
| Chain | Residue |
| A | ASP120 |
| A | CYS198 |
| A | HIS240 |
| A | ZN351 |
| A | HOH2117 |
| A | HOH2192 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 351 |
| Chain | Residue |
| A | HIS116 |
| A | HIS118 |
| A | HIS179 |
| A | ZN350 |
| A | HOH2117 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20677753","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24059435","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7588620","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9761898","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20677753","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24059435","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9761898","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 16 |
| Chain | Residue | Details |
| A | HIS116 | metal ligand |
| A | HIS118 | metal ligand |
| A | ASP120 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | HIS179 | metal ligand |
| A | ASN210 | electrostatic stabiliser, hydrogen bond donor |
