1xi6

X-ray diffraction
2.8Å resolution

Extragenic suppressor from Pyrococcus furiosus Pfu-1862794-001

Released:
Source organism: Pyrococcus furiosus
Entry authors: Zhao M, Chang JC, Zhou W, Chen L, Horanyi P, Xu H, Yang H, Liu Z-J, Habel JE, Lee D, Chang S-H, Rose JP, Wang B-C, Southeast Collaboratory for Structural Genomics (SECSG)

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:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-186325 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-1,6-bisphosphatase Chain: A
Molecule details ›
Chain: A
Length: 262 amino acids
Theoretical weight: 28.88 KDa
Source organism: Pyrococcus furiosus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8TZH9 (Residues: 2-254; Coverage: 100%)
Gene names: PF2014, fbp, fbpA
Sequence domains: Inositol monophosphatase family
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: I4122
Unit cell:
a: 81.613Å b: 81.613Å c: 293.871Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.272 0.271 0.298
Expression system: Escherichia coli