› 1o6c

X-ray diffraction
2.9Å resolution

Function and Biology Details

Reaction catalysed: 
UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-mannosamine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153841 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetylglucosamine 2-epimerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 388 amino acids
Theoretical weight: 44.14 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P39131 (Residues: 2-380; Coverage: 100%)
Gene names: BSU35660, mnaA
Sequence domains: UDP-N-acetylglucosamine 2-epimerase
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 20 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: P43212
Unit cell:
a: 63.82Å b: 63.82Å c: 452.43Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.274 0.274 0.334
Expression system: Escherichia coli

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Citations

23 review citations

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

4 mentions without citation

A structural basis for the allosteric regulation of non-hydrolysing UDP-GlcNAc 2-epimerases.
Velloso et al. (2008)
3 more