› 6skq

X-ray diffraction
2.1Å resolution

OXA-655_MEM. Structural insights into the enhanced carbapenemase efficiency of OXA-655 compared to OXA-10.

Released:
DOI: 10.2210/pdb6skq/pdb
PDB entry 6skq coloured by chain, front view.
PDB entry 6skq coloured by chain, side view.
PDB entry 6skq coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural insights into the enhanced carbapenemase efficiency of OXA-655 compared to OXA-10.
Leiros HS, Thomassen AM, Samuelsen Ø, Flach CF, Kotsakis SD, Larsson DGJ
OpenAccess logo FEBS Open Bio 10 1821-1832 (2020)
PMID: 32683794

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-104767 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 266 amino acids
Theoretical weight: 29.63 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A386YIZ1 (Residues: 1-266; Coverage: 100%)
Gene names: blaOXA, blaOXA-655
Sequence domains: Penicillin binding protein transpeptidase domain

Ligands and Environments

2 bound ligands:
Ligand MER 4 x MER
Ligand SO4 5 x SO4
1 modified residue:
Ligand KCX 4 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P21
Unit cell:
a: 68.137Å b: 82.437Å c: 99.004Å
α: 90° β: 97.007° γ: 90°
R-values:
R R work R free
0.182 0.179 0.235
Expression system: Escherichia coli

Quick links

Citations

1 review citation

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

4 mentions without citation

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