› 3fbp

X-ray diffraction
2.8Å resolution

STRUCTURE REFINEMENT OF FRUCTOSE-1,6-BISPHOSPHATASE AND ITS FRUCTOSE 2,6-BISPHOSPHATE COMPLEX AT 2.8 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb3fbp/pdb
PDB entry 3fbp coloured by chain, front view.
PDB entry 3fbp coloured by chain, side view.
PDB entry 3fbp coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Structure refinement of fructose-1,6-bisphosphatase and its fructose 2,6-bisphosphate complex at 2.8 A resolution.
Ke HM, Thorpe CM, Seaton Ba, Lipscomb WN, Marcus F
J Mol Biol 212 513-39 (1990)
PMID: 2157849

Function and Biology Details

Reaction catalysed: 
D-fructose 1,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132778 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-1,6-bisphosphatase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 335 amino acids
Theoretical weight: 36.5 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
  • Canonical: P00636 (Residues: 2-336; Coverage: 99%)
Gene names: FBP, FBP1
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand FDP 2 x FDP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 131.6Å b: 131.6Å c: 68.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.188 not available
Expression system: Not provided

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Citations

31 citation in other articles

Similarities and differences between human cyclophilin A and other beta-barrel structures. Structural refinement at 1.63 A resolution.
Ke H. (1992)
30 more