› 1nv4

X-ray diffraction
1.9Å resolution

Fructose-1,6-Bisphosphatase Complex with Magnesium, Fructose-6-Phosphate, Phosphate, EDTA and Thallium (1 mM)

Released:
DOI: 10.2210/pdb1nv4/pdb
PDB entry 1nv4 coloured by chain, front view.
PDB entry 1nv4 coloured by chain, side view.
PDB entry 1nv4 coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Interaction of Tl+ with product complexes of fructose-1,6-bisphosphatase.
Choe JY, Nelson SW, Fromm HJ, Honzatko RB
J Biol Chem 278 16008-14 (2003)
PMID: 12595529

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

Assemblies composition:
monomeric (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-523720 (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

4 bound ligands:
Ligand F6P 1 x F6P
Ligand MG 2 x MG
Ligand PO4 2 x PO4
Ligand TL 3 x TL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: I222
Unit cell:
a: 53.074Å b: 82.829Å c: 165.173Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.184 0.236
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

The first crystal structure of the novel class of fructose-1,6-bisphosphatase present in thermophilic archaea.
Nishimasu et al. (2004)
4 more