5ky6

X-ray diffraction
1.94Å resolution

Human muscle fructose-1,6-bisphosphate aldolase

Released:
Source organism: Homo sapiens
Entry authors: Wisniewski J, Barciszewski J, Jaskolski M, Rakus D

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)
PDBe Complex ID:
PDB-CPX-137391 (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: 39.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P04075 (Residues: 2-364; Coverage: 100%)
Gene names: ALDA, ALDOA
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
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P21
Unit cell:
a: 84.511Å b: 57.253Å c: 164.016Å
α: 90° β: 102.57° γ: 90°
R-values:
R R work R free
0.187 0.186 0.223
Expression system: Escherichia coli BL21