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 octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133668 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Fructose-bisphosphate aldolase A
Molecule details ›
Chains: A, B, C, D
Length: 363 amino acids
Theoretical weight: 39.26 KDa
Source organism: Oryctolagus cuniculus
Expression system: Escherichia coli
UniProt:
Sequence domains: Fructose-bisphosphate aldolase class-I
Structure domains: Aldolase class I
Length: 363 amino acids
Theoretical weight: 39.26 KDa
Source organism: Oryctolagus cuniculus
Expression system: Escherichia coli
UniProt:
- Canonical:
P00883 (Residues: 2-364; Coverage: 100%)
Sequence domains: Fructose-bisphosphate aldolase class-I
Structure domains: Aldolase class I
Sorting nexin-9
Molecule details ›
Chains: E, F, G, H
Length: 31 amino acids
Theoretical weight: 3.51 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
Length: 31 amino acids
Theoretical weight: 3.51 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
- Canonical: Q9Y5X1 (Residues: 152-182; Coverage: 5%)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 22-BM
Spacegroup:
P212121
Expression systems:
- Escherichia coli
- Not provided
