› 1fpk

X-ray diffraction
3Å resolution

FRUCTOSE-1,6-BISPHOSPHATASE (D-FRUCTOSE-1,6-BISPHOSPHATE 1-PHOSPHOHYDROLASE) COMPLEXED WITH THALLIUM IONS (10 MM)

Released:
DOI: 10.2210/pdb1fpk/pdb
PDB entry 1fpk coloured by chain, front view.
PDB entry 1fpk coloured by chain, side view.
PDB entry 1fpk coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Crystallographic evidence for the action of potassium, thallium, and lithium ions on fructose-1,6-bisphosphatase.
Villeret V, Huang S, Fromm HJ, Lipscomb WN
Proc Natl Acad Sci U S A 92 8916-20 (1995)
PMID: 7568043

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
UniProt:
  • Canonical: P00636 (Residues: 2-336; Coverage: 99%)
Gene names: FBP, FBP1
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand TL 6 x TL
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 132.6Å b: 132.6Å c: 67.7Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.226 0.226 not available

Quick links

Citations

10 review citations

Molecular targets of lithium action.
Phiel et al. (2001)
9 more

1 mention without citation

A structural basis for lithium and substrate binding of an inositide phosphatase.
Dollins et al. (2021)