X-ray diffraction
2.37Å resolution

Crystal structure of fructose bisphosphate aldolase from Encephalitozoon cuniculi, bound to fructose 1,6-bisphosphate

Source organism: Encephalitozoon cuniculi
Primary publication:
Structure of fructose bisphosphate aldolase from Encephalitozoon cuniculi.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67 1055-9 (2011)
PMID: 21904050

Function and Biology Details

Reaction catalysed:
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Fructose-bisphosphate aldolase Chain: A
Molecule details ›
Chain: A
Length: 342 amino acids
Theoretical weight: 38.26 KDa
Source organism: Encephalitozoon cuniculi
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q8SSM8 (Residues: 1-338; Coverage: 100%)
Gene name: ECU01_0240
Sequence domains: Fructose-bisphosphate aldolase class-I
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: C2221
Unit cell:
a: 121.46Å b: 135.82Å c: 61.54Å
α: 90° β: 90° γ: 90°
R R work R free
0.167 0.165 0.208
Expression system: Escherichia coli BL21(DE3)