› 4k0x

X-ray diffraction
1.61Å resolution

X-ray Crystal Structure of OXA-23 from Acinetobacter baumannii

Released:
DOI: 10.2210/pdb4k0x/pdb
PDB entry 4k0x coloured by chain, front view.
PDB entry 4k0x coloured by chain, side view.
PDB entry 4k0x 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-192203 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Penicillin-binding protein transpeptidase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 243 amino acids
Theoretical weight: 27.69 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9L4P2 (Residues: 31-273; Coverage: 89%)
Gene names: A7M90_19440, ABUW_0563, B9W25_19205, CAS83_19595, CBE85_20255, EA686_06705, F2P40_21140, G3N53_19695, GNY86_20740, IAG11_18825, ITE13_20155, JHZ39_003791, JHZ39_003875, NG19_0098, OXA-23, SAMEA104305318_04148, SAMEA4394745_03802, ari-1, bla(OXA-23), bla-OXA-23, bla-oxa-23, blaOXA, blaOXA-23, bla_3, oxa-23, oxa23
Sequence domains: Penicillin binding protein transpeptidase domain
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
Ligand BCT 2 x BCT
1 modified residue:
Ligand KCX 1 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Unit cell:
a: 44Å b: 46.539Å c: 136.852Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.164 0.192
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

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

9 mentions without citation

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