1xfb

X-ray diffraction
3Å resolution

Human Brain Fructose 1,6-(bis)phosphate Aldolase (C isozyme)

Released:

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-140871 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-bisphosphate aldolase C Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 365 amino acids
Theoretical weight: 39.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09972 (Residues: 1-364; Coverage: 100%)
Gene names: ALDC, ALDOC
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: RIGAKU RU300
Spacegroup: P1
Unit cell:
a: 83.872Å b: 121.986Å c: 129.517Å
α: 107.96° β: 108.58° γ: 97.39°
R-values:
R R work R free
0.257 0.255 0.261
Expression system: Escherichia coli