4zht

X-ray diffraction
2.69Å resolution

Crystal structure of UDP-GlcNAc 2-epimerase

Released:

Function and Biology Details

Reactions catalysed:
ATP + N-acyl-D-mannosamine = ADP + N-acyl-D-mannosamine 6-phosphate
UDP-N-acetyl-alpha-D-glucosamine + H(2)O = N-acetyl-D-mannosamine + UDP
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-195079 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 411 amino acids
Theoretical weight: 47.08 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9Y223 (Residues: 1-405; Coverage: 56%)
Gene names: GLCNE, GNE, IBM2
Sequence domains: UDP-N-acetylglucosamine 2-epimerase

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: C2
Unit cell:
a: 106.041Å b: 98.102Å c: 154.722Å
α: 90° β: 96.05° γ: 90°
R-values:
R R work R free
0.191 0.189 0.225
Expression system: Escherichia coli BL21