› 5fbp

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURE OF THE NEUTRAL FORM OF FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH THE PRODUCT FRUCTOSE 6-PHOSPHATE AT 2.1-ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb5fbp/pdb
PDB entry 5fbp coloured by chain, front view.
PDB entry 5fbp coloured by chain, side view.
PDB entry 5fbp coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Crystal structure of the neutral form of fructose-1,6-bisphosphatase complexed with the product fructose 6-phosphate at 2.1-A resolution.
Ke HM, Zhang YP, Liang JY, Lipscomb WN
Proc Natl Acad Sci U S A 88 2989-93 (1991)
PMID: 1849642

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: 335 amino acids
Theoretical weight: 36.5 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
  • Canonical: P00636 (Residues: 2-336; Coverage: 99%)
Gene names: FBP, FBP1
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand F6P 3 x F6P
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 131.1Å b: 131.1Å c: 69.7Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.177 0.177 not available
Expression system: Not provided

Quick links

Citations

1 review citation

Localization and regulation of muscle fructose-1,6-bisphosphatase, the key enzyme of glyconeogenesis.
Dzugaj A. (2006)
26 other articles

2 mentions without citation

Overview of protein structural and functional folds.
Sun et al. (2004)
1 more