› 4x56

X-ray diffraction
2.28Å resolution

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Penicillin-binding protein transpeptidase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 245 amino acids
Theoretical weight: 27.68 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: D2XKK9 (Residues: 31-275; Coverage: 97%)
Gene name: blaOXA-160
Sequence domains: Penicillin binding protein transpeptidase domain
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
Ligand CAZ 1 x CAZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P41212
Unit cell:
a: 102.307Å b: 102.307Å c: 87.151Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.181 0.213
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

β-Lactam antibiotic targets and resistance mechanisms: from covalent inhibitors to substrates.
Mora-Ochomogo et al. (2021)
11 other articles

4 mentions without citation

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