› 2qvu

X-ray diffraction
1.5Å resolution

Porcine Liver Fructose-1,6-bisphosphatase cocrystallized with Fru-2,6-P2 and Mg2+, I(T)-state

Released:
DOI: 10.2210/pdb2qvu/pdb
PDB entry 2qvu coloured by chain, front view.
PDB entry 2qvu coloured by chain, side view.
PDB entry 2qvu coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Structures of mammalian and bacterial fructose-1,6-bisphosphatase reveal the basis for synergism in AMP/fructose 2,6-bisphosphate inhibition.
Hines JK, Chen X, Nix JC, Fromm HJ, Honzatko RB
J Biol Chem 282 36121-31 (2007)
PMID: 17933867

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: 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:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand FDP 2 x FDP
Ligand PO4 2 x PO4
Ligand MG 4 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P21212
Unit cell:
a: 59.173Å b: 165.627Å c: 79.618Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.196 0.214
Expression system: Escherichia coli

Quick links

Citations

11 citation in other articles

Rational engineering of enzyme allosteric regulation through sequence evolution analysis.
Yang et al. (2012)
10 more

1 mention without citation

Central cavity of fructose-1,6-bisphosphatase and the evolution of AMP/fructose 2,6-bisphosphate synergism in eukaryotic organisms.
Gao et al. (2014)