2f3d

X-ray diffraction
1.83Å resolution

Mechanism of displacement of a catalytically essential loop from the active site of fructose-1,6-bisphosphatase

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
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: 338 amino acids
Theoretical weight: 36.82 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli
UniProt:
  • Canonical: P00636 (Residues: 1-338; Coverage: 100%)
Gene names: FBP, FBP1
Sequence domains:
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: I222
Unit cell:
a: 55.84Å b: 82.502Å c: 165.025Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.222 0.246
Expression system: Escherichia coli