› 6pk0

X-ray diffraction
1.75Å resolution

Crystal Structure of OXA-48 with Hydrolyzed Imipenem

Released:
DOI: 10.2210/pdb6pk0/pdb
PDB entry 6pk0 coloured by chain, front view.
PDB entry 6pk0 coloured by chain, side view.
PDB entry 6pk0 coloured by chain, top view.
Source organism: Klebsiella pneumoniae
Primary publication:
Structural Basis for Substrate Specificity and Carbapenemase Activity of OXA-48 Class D β-Lactamase.
Akhtar A, Pemberton OA, Chen Y
ACS Infect Dis 6 261-271 (2020)
PMID: 31872762

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180524 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 263 amino acids
Theoretical weight: 30.87 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6XEC0 (Residues: 3-3, 25-265; Coverage: 91%)
Gene names: BANRA_05332, BV369_20085, GJJ01_28680, KPE71T_00045, SAMEA3729652_05148, bla OXA-48, blaOXA-48, bla_4
Sequence domains: Penicillin binding protein transpeptidase domain

Ligands and Environments

3 bound ligands:
Ligand HIW 5 x HIW
Ligand CL 2 x CL
Ligand GOL 6 x GOL
1 modified residue:
Ligand KCX 4 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P21
Unit cell:
a: 58.05Å b: 105.43Å c: 93.57Å
α: 90° β: 107.96° γ: 90°
R-values:
R R work R free
0.162 0.159 0.202
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 citation in other articles

Analysis of β-lactone formation by clinically observed carbapenemases informs on a novel antibiotic resistance mechanism.
Aertker et al. (2020)
7 more

2 mentions without citation

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