› 1nuw

X-ray diffraction
1.3Å resolution

Fructose-1,6-Bisphosphatase Complex with Magnesium, Fructose-6-Phosphate and Phosphate at pH 9.6

Released:
DOI: 10.2210/pdb1nuw/pdb
PDB entry 1nuw coloured by chain, front view.
PDB entry 1nuw coloured by chain, side view.
PDB entry 1nuw coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Metaphosphate in the active site of fructose-1,6-bisphosphatase.
Choe JY, Iancu CV, Fromm HJ, Honzatko RB
J Biol Chem 278 16015-20 (2003)
PMID: 12595528

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-132776 (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 PO3 1 x PO3
Ligand MG 4 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: I222
Unit cell:
a: 53.6Å b: 83.017Å c: 165.378Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.164 0.207
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Mechanism and applications of phosphite dehydrogenase.
Relyea et al. (2005)
1 more

2 mentions without citation

Crystal structures of human muscle fructose-1,6-bisphosphatase: novel quaternary states, enhanced AMP affinity, and allosteric signal transmission pathway.
Shi et al. (2013)
1 more