› 4k0w

X-ray diffraction
1.2Å resolution

X-ray crystal structure of OXA-23 A220 duplication clinical variant

Released:
DOI: 10.2210/pdb4k0w/pdb
PDB entry 4k0w coloured by chain, front view.
PDB entry 4k0w coloured by chain, side view.
PDB entry 4k0w coloured by chain, top view.
Source organism: Acinetobacter baumannii
Primary publication:
Structures of the class D Carbapenemases OXA-23 and OXA-146: mechanistic basis of activity against carbapenems, extended-spectrum cephalosporins, and aztreonam.
Kaitany KC, Klinger NV, June CM, Ramey ME, Bonomo RA, Powers RA, Leonard DA
Antimicrob Agents Chemother 57 4848-55 (2013)
PMID: 23877677

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-110327 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Penicillin-binding protein transpeptidase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 244 amino acids
Theoretical weight: 27.72 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B6E129 (Residues: 31-219, 221-274; Coverage: 89%)
Gene name: blaOXA-146
Sequence domains: Penicillin binding protein transpeptidase domain
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

4 bound ligands:
Ligand CIT 1 x CIT
Ligand EDO 4 x EDO
Ligand BCT 4 x BCT
Ligand NA 5 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Unit cell:
a: 44.116Å b: 46.662Å c: 137.018Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.182 0.202
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

OXA β-lactamases.
Evans et al. (2014)
12 more

5 mentions without citation

Structural basis for carbapenem-hydrolyzing mechanisms of carbapenemases conferring antibiotic resistance.
Jeon et al. (2015)
4 more