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:
Fructose-bisphosphate aldolase (preferred)
PDBe Complex ID:
PDB-CPX-146884 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-bisphosphate aldolase
Molecule details ›
Chains: A, B
Length: 368 amino acids
Theoretical weight: 40.02 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
UniProt:
Sequence domains: Fructose-bisphosphate aldolase class-I
Structure domains: Aldolase class I
Length: 368 amino acids
Theoretical weight: 40.02 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
UniProt:
- Canonical:
P14223 (Residues: 2-369; Coverage: 100%)
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
X-ray source:
ESRF BEAMLINE BM02
Spacegroup:
P3221
Expression system: Escherichia coli
