4Y0O
Crystal structure of OXA-58, a carbapenem hydrolyzing Class D beta-lactamase from Acinetobacter baumanii.
Functional Information from GO Data
Functional Information from PROSITE/UniProt
site_id | PS00337 |
Number of Residues | 11 |
Details | BETA_LACTAMASE_D Beta-lactamase class-D active site. PaSTFKIAnAL |
Chain | Residue | Details |
A | PRO81-LEU91 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | Active site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PIRSR","id":"PIRSR602137-50","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26459904","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4Y0U","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"26459904","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4Y0U","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P13661","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q8RLA6","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PIRSR","id":"PIRSR602137-50","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24468777","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26459904","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26701320","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4OH0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4Y0O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4Y0T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4Y0U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5BOH","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |