› 6p9c

X-ray diffraction
1.9Å resolution

OXA-48 carbapanemase, doripenem complex

Released:
DOI: 10.2210/pdb6p9c/pdb
PDB entry 6p9c coloured by chain, front view.
PDB entry 6p9c coloured by chain, side view.
PDB entry 6p9c coloured by chain, top view.
Source organism: Klebsiella pneumoniae
Primary publication:
Structural Insights into the Mechanism of Carbapenemase Activity of the OXA-48 β-Lactamase.
Smith CA, Stewart NK, Toth M, Vakulenko SB
Antimicrob Agents Chemother 63 (2019)
PMID: 31358584

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180526 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chains: A, B
Molecule details ›
Chains: A, B
Length: 265 amino acids
Theoretical weight: 30.4 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6XEC0 (Residues: 1-265; Coverage: 100%)
Gene names: KPE71T_00045, bla OXA-48, blaOXA-48
Sequence domains: Penicillin binding protein transpeptidase domain

Ligands and Environments

5 bound ligands:
Ligand 4J6 2 x 4J6
Ligand O6P 2 x O6P
Ligand CL 4 x CL
Ligand CA 3 x CA
Ligand CD 2 x CD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: P212121
Unit cell:
a: 72.604Å b: 76.749Å c: 101.188Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.194 0.241
Expression system: Escherichia coli

Quick links

Citations

4 review citations

A review on the mechanistic details of OXA enzymes of ESKAPE pathogens.
Avci et al. (2023)
3 more

5 mentions without citation

Antimicrobial Resistance Conferred by OXA-48 β-Lactamases: Towards a Detailed Mechanistic Understanding.
Hirvonen et al. (2021)
4 more