› 1eyi

X-ray diffraction
2.32Å resolution

FRUCTOSE-1,6-BISPHOSPHATASE COMPLEX WITH MAGNESIUM, FRUCTOSE-6-PHOSPHATE AND PHOSPHATE (R-STATE)

Released:
DOI: 10.2210/pdb1eyi/pdb
PDB entry 1eyi coloured by chain, front view.
PDB entry 1eyi coloured by chain, side view.
PDB entry 1eyi 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 Chain: A
Molecule details ›
Chain: A
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 F6P 1 x F6P
Ligand MG 2 x MG
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: I222
Unit cell:
a: 52.12Å b: 82.51Å c: 165.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.19 0.242
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

8 mentions without citation

Prediction of catalytic residues using Support Vector Machine with selected protein sequence and structural properties.
Petrova et al. (2006)
7 more