› 1fbe

X-ray diffraction
3Å resolution

CRYSTALLOGRAPHIC STUDIES OF THE CATALYTIC MECHANISM OF THE NEUTRAL FORM OF FRUCTOSE-1,6-BISPHOSPHATASE

Released:
DOI: 10.2210/pdb1fbe/pdb
PDB entry 1fbe coloured by chain, front view.
PDB entry 1fbe coloured by chain, side view.
PDB entry 1fbe coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Crystallographic studies of the catalytic mechanism of the neutral form of fructose-1,6-bisphosphatase.
Zhang Y, Liang JY, Huang S, Ke H, Lipscomb WN
Biochemistry 32 1844-57 (1993)
PMID: 8382525

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

2 bound ligands:
Ligand ZN 4 x ZN
Ligand AHG 2 x AHG
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 132Å b: 132Å c: 67.4Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.195 not available
Expression system: Not provided

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Citations

6 review citations

Zinc enzymes.
Coleman JE. (1998)
5 more