PDBe 2qut

X-ray diffraction
1.88Å resolution

Dihydroxyacetone phosphate enamine intermediate in fructose-1,6-bisphosphate aldolase from rabbit muscle

Released:

Function and Biology Details

Reaction catalysed:
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. 
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-bisphosphate aldolase A Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 363 amino acids
Theoretical weight: 39.26 KDa
Source organism: Oryctolagus cuniculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00883 (Residues: 2-364; Coverage: 100%)
Gene name: ALDOA
Sequence domains: Fructose-bisphosphate aldolase class-I
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: P21
Unit cell:
a: 82.77Å b: 102.912Å c: 84.235Å
α: 90° β: 98.483° γ: 90°
R-values:
R R work R free
0.159 0.159 0.191
Expression system: Escherichia coli