› 6rj7

X-ray diffraction
1.73Å resolution

Crystal structure of the 19F labelled OXA-48

Released:
DOI: 10.2210/pdb6rj7/pdb
PDB entry 6rj7 coloured by chain, front view.
PDB entry 6rj7 coloured by chain, side view.
PDB entry 6rj7 coloured by chain, top view.
Source organism: Klebsiella pneumoniae
Primary publication:
19 F NMR Monitoring of Reversible Protein Post-Translational Modifications: Class D β-Lactamase Carbamylation and Inhibition.
van Groesen E, Lohans CT, Brem J, Aertker KMJ, Claridge TDW, Schofield CJ
Chemistry 25 11837-11841 (2019)
PMID: 31310409

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: 245 amino acids
Theoretical weight: 28.58 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q6XEC0 (Residues: 23-265; Coverage: 100%)
Gene names: KPE71T_00045, bla OXA-48, blaOXA-48
Sequence domains: Penicillin binding protein transpeptidase domain

Ligands and Environments

2 bound ligands:
Ligand CL 1 x CL
Ligand CA 1 x CA
2 modified residues:
Ligand KCX 2 x KCX
Ligand K5H 2 x K5H

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P21
Unit cell:
a: 64.36Å b: 58.03Å c: 66.43Å
α: 90° β: 91.49° γ: 90°
R-values:
R R work R free
0.179 0.177 0.21
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

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

1 mention without citation

19 F NMR Monitoring of Reversible Protein Post-Translational Modifications: Class D β-Lactamase Carbamylation and Inhibition.
van Groesen et al. (2019)