› 1fba

X-ray diffraction
1.9Å resolution

THE CRYSTAL STRUCTURE OF FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE FROM DROSOPHILA MELANOGASTER AT 2.5 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1fba/pdb
PDB entry 1fba coloured by chain, front view.
PDB entry 1fba coloured by chain, side view.
PDB entry 1fba coloured by chain, top view.
Source organism: Drosophila melanogaster
Primary publication:
The crystal structure of fructose-1,6-bisphosphate aldolase from Drosophila melanogaster at 2.5 A resolution.
Hester G, Brenner-Holzach O, Rossi FA, Struck-Donatz M, Winterhalter KH, Smit JD, Piontek K
FEBS Lett 292 237-42 (1991)
PMID: 1959612

Function and Biology Details

Reaction catalysed: 
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-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-139747 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-bisphosphate aldolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 361 amino acids
Theoretical weight: 38.99 KDa
Source organism: Drosophila melanogaster
Expression system: Not provided
UniProt:
  • Canonical: P07764 (Residues: 2-361; Coverage: 100%)
Gene names: Ald1, CG6058
Sequence domains: Fructose-bisphosphate aldolase class-I
Structure domains: Aldolase class I

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 86.6Å b: 116.8Å c: 151.58Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 not available not available
Expression system: Not provided

Quick links

Citations

6 review citations

Evolution of glycolysis.
Fothergill-Gilmore et al. (1993)
5 more

3 mentions without citation

"Hidden" sequence periodicities and protein architecture.
Rackovsky S. (1998)
2 more