PDBe 1qo5

X-ray diffraction
2.5Å resolution

Fructose 1,6-bisphosphate Aldolase from Human Liver Tissue

Released:
Source organism: Homo sapiens
Primary publication:
The structure of human liver fructose-1,6-bisphosphate aldolase.
Acta Crystallogr. D Biol. Crystallogr. 57 1526-33 (2001)
PMID: 11679716

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-bisphosphate aldolase B Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R
Length: 363 amino acids
Theoretical weight: 39.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P05062 (Residues: 2-364; Coverage: 100%)
Gene names: ALDB, ALDOB
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: SRS BEAMLINE PX9.5
Spacegroup: C2
Unit cell:
a: 291.1Å b: 489.84Å c: 103.36Å
α: 90° β: 103.68° γ: 90°
R-values:
R R work R free
0.224 0.224 0.276
Expression system: Escherichia coli