› 1eyk

X-ray diffraction
2.23Å resolution

FRUCTOSE-1,6-BISPHOSPHATASE COMPLEX WITH AMP, ZINC, FRUCTOSE-6-PHOSPHATE AND PHOSPHATE (T-STATE)

Released:
DOI: 10.2210/pdb1eyk/pdb
PDB entry 1eyk coloured by chain, front view.
PDB entry 1eyk coloured by chain, side view.
PDB entry 1eyk coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Crystal structures of fructose 1,6-bisphosphatase: mechanism of catalysis and allosteric inhibition revealed in product complexes.
Choe JY, Fromm HJ, Honzatko RB
Biochemistry 39 8565-74 (2000)
PMID: 10913263

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

4 bound ligands:
Ligand F6P 2 x F6P
Ligand ZN 2 x ZN
Ligand PO4 2 x PO4
Ligand AMP 2 x AMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: P21212
Unit cell:
a: 60.12Å b: 166.14Å c: 79.53Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.217 0.271
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Structural and mechanistic insights into the bifunctional enzyme isocitrate dehydrogenase kinase/phosphatase AceK.
Zheng et al. (2012)
1 more

5 mentions without citation

Designing inhibitors against fructose 1,6-bisphosphatase: exploring natural products for novel inhibitor scaffolds.
Heng et al. (2010)
4 more