PDBe 1umg

X-ray diffraction
1.8Å resolution

Crystal structure of fructose-1,6-bisphosphatase

Released:

Function and Biology Details

Reactions catalysed:
D-fructose 1,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-1,6-bisphosphate aldolase/phosphatase Chain: A
Molecule details ›
Chain: A
Length: 362 amino acids
Theoretical weight: 40.1 KDa
Source organism: Sulfolobus tokodaii str. 7
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: F9VMT6 (Residues: 2-363; Coverage: 94%)
Gene names: STK_03180, fbp
Sequence domains: Fructose-1,6-bisphosphatase

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL40B2
Spacegroup: I422
Unit cell:
a: 111.778Å b: 111.778Å c: 153.174Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.183 0.197
Expression system: Escherichia coli BL21(DE3)