› 6n6t

X-ray diffraction
1.25Å resolution

OXA-23 mutant F110A/M221A low pH form

Released:
DOI: 10.2210/pdb6n6t/pdb
Model geometry
Data not analysed
Fit model/data
Data not analysed
PDB entry 6n6t coloured by chain, front view.
PDB entry 6n6t coloured by chain, side view.
PDB entry 6n6t coloured by chain, top view.
Source organism: Acinetobacter baumannii
Primary publication:
Role of the Hydrophobic Bridge in the Carbapenemase Activity of Class D β-Lactamases.
Stewart NK, Smith CA, Antunes NT, Toth M, Vakulenko SB
Antimicrob Agents Chemother 63 (2019)
PMID: 30530607

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
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:
Beta-lactamase OXA-23 Chain: A
Molecule details ›
Chain: A
Length: 243 amino acids
Theoretical weight: 27.51 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9L4P2 (Residues: 31-273; Coverage: 95%)
Gene names: ABUW_0563, OXA-23, ari-1, bla-OXA-23, blaOXA, blaOXA-23, bla_2, bla_3
Sequence domains: Penicillin binding protein transpeptidase domain
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

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

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P21212
Unit cell:
a: 136.581Å b: 43.991Å c: 46.552Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.156 0.154 0.18
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)
17 other articles

1 mention without citation

Role of the Hydrophobic Bridge in the Carbapenemase Activity of Class D β-Lactamases.
Stewart et al. (2019)