› 1o69

X-ray diffraction
1.84Å resolution

Function and Biology Details

Reaction catalysed: 
UDP-N-acetylbacillosamine + 2-oxoglutarate = UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose + L-glutamate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193413 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminotransferase homolog Chains: A, B
Molecule details ›
Chains: A, B
Length: 394 amino acids
Theoretical weight: 44.81 KDa
Source organism: Campylobacter jejuni
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9S5Y7 (Residues: 1-386; Coverage: 100%)
Gene names: BFD99_05430, QQI97_000131, pglE
Sequence domains: DegT/DnrJ/EryC1/StrS aminotransferase family
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand X04 2 x X04
Ligand BME 2 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: P65
Unit cell:
a: 151.774Å b: 151.774Å c: 76.986Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.185 0.185 0.225
Expression system: Escherichia coli

Quick links

Citations

23 review citations

Regulation of fatty acid metabolism in bacteria.
Fujita et al. (2007)
22 more

3 mentions without citation

Structure of the external aldimine form of PglE, an aminotransferase required for N,N'-diacetylbacillosamine biosynthesis.
Riegert et al. (2015)
2 more