PDBe 4he0

X-ray diffraction
2.69Å resolution

Crystal structure of human muscle fructose-1,6-bisphosphatase

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 isozyme 2 Chain: A
Molecule details ›
Chain: A
Length: 338 amino acids
Theoretical weight: 36.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O00757 (Residues: 2-339; Coverage: 100%)
Gene name: FBP2
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: RIGAKU RU200
Spacegroup: P42212
Unit cell:
a: 73.853Å b: 73.853Å c: 146.749Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.2 0.253
Expression system: Escherichia coli BL21(DE3)