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:
hetero pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-243742 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Fructose-bisphosphate aldolase
Molecule details ›
Chains: A, B, C, D
Length: 369 amino acids
Theoretical weight: 40.15 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
UniProt:
Sequence domains: Fructose-bisphosphate aldolase class-I
Structure domains: Aldolase class I
Length: 369 amino acids
Theoretical weight: 40.15 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
UniProt:
- Canonical:
P14223 (Residues: 1-369; Coverage: 100%)
Sequence domains: Fructose-bisphosphate aldolase class-I
Structure domains: Aldolase class I
Thrombospondin-related anonymous protein
Molecule details ›
Chain: H
Length: 6 amino acids
Theoretical weight: 792 Da
Source organism: Plasmodium berghei
Expression system: Not provided
UniProt:
Length: 6 amino acids
Theoretical weight: 792 Da
Source organism: Plasmodium berghei
Expression system: Not provided
UniProt:
- Canonical: P90573 (Residues: 601-606; Coverage: 1%)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ALS BEAMLINE 8.2.2
Spacegroup:
P212121
Expression systems:
- Escherichia coli
- Not provided
