PDBe 1eyi

X-ray diffraction
2.32Å resolution

FRUCTOSE-1,6-BISPHOSPHATASE COMPLEX WITH MAGNESIUM, FRUCTOSE-6-PHOSPHATE AND PHOSPHATE (R-STATE)

Released:

Function and Biology Details

Reaction catalysed:
D-fructose 1,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate. 
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-1,6-bisphosphatase 1 Chain: A
Molecule details ›
Chain: A
Length: 337 amino acids
Theoretical weight: 36.69 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli
UniProt:
  • Canonical: P00636 (Residues: 2-338; Coverage: 100%)
Gene names: FBP, FBP1
Sequence domains: Fructose-1-6-bisphosphatase, N-terminal domain
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: I222
Unit cell:
a: 52.12Å b: 82.51Å c: 165.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.19 0.242
Expression system: Escherichia coli