5FQB
Crystal Structure of Bacillus cereus Metallo-Beta-Lactamase with 2C
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 | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 295 |
| Chain | Residue |
| A | ASP123 |
| A | CYS224 |
| A | HIS266 |
| A | OK3297 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 296 |
| Chain | Residue |
| A | HIS119 |
| A | HIS121 |
| A | HIS199 |
| A | OK3297 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE OK3 A 297 |
| Chain | Residue |
| A | TRP90 |
| A | HIS119 |
| A | HIS121 |
| A | ALA122 |
| A | ASP123 |
| A | HIS199 |
| A | CYS224 |
| A | LYS227 |
| A | ASN236 |
| A | ASP239 |
| A | HIS266 |
| A | ZN295 |
| A | ZN296 |
| A | HOH2120 |
| A | HOH2132 |
| A | HOH2150 |
| A | PHE65 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 298 |
| Chain | Residue |
| A | LYS105 |
| A | LYS189 |
| A | GLN213 |
| A | HOH2126 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 299 |
| Chain | Residue |
| A | GLU100 |
| A | GLU133 |
| A | ARG134 |
| A | HOH2190 |
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 | HIS119 | metal ligand |
| A | HIS121 | metal ligand |
| A | ASP123 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | HIS199 | metal ligand |
| A | ASN236 | electrostatic stabiliser, hydrogen bond donor |
