4utu

X-ray diffraction
1.45Å resolution

Structural and biochemical characterization of the N- acetylmannosamine-6-phosphate 2-epimerase from Clostridium perfringens

Released:
Entry authors: Pelissier MC, Sebban-Kreuzer C, Guerlesquin F, Brannigan JA, Davies GJ, Bourne Y, Vincent F

Function and Biology Details

Reaction catalysed:
N-acyl-D-glucosamine 6-phosphate = N-acyl-D-mannosamine 6-phosphate
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative N-acetylmannosamine-6-phosphate 2-epimerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 229 amino acids
Theoretical weight: 25.06 KDa
Source organism: Clostridium perfringens str. 13
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8XNZ3 (Residues: 1-220; Coverage: 100%)
Gene names: CPE0184, nanE, nanP
Sequence domains: Putative N-acetylmannosamine-6-phosphate epimerase
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 36.714Å b: 82.147Å c: 75.195Å
α: 90° β: 92.48° γ: 90°
R-values:
R R work R free
0.141 0.14 0.169
Expression system: Escherichia coli BL21(DE3)