› 4jf4

X-ray diffraction
2.14Å resolution

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 243 amino acids
Theoretical weight: 27.65 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli
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

2 bound ligands:
Ligand EDO 1 x EDO
Ligand MER 2 x MER
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: P21
Unit cell:
a: 49.467Å b: 44.533Å c: 131.367Å
α: 90° β: 94.93° γ: 90°
R-values:
R R work R free
0.202 0.199 0.254
Expression system: Escherichia coli

Quick links

Citations

13 review citations

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

28 mentions without citation

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