Function and Biology Details
Reaction catalysed:
Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Transaldolase (preferred)
PDBe Complex ID:
PDB-CPX-153494 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transaldolase
Molecule details ›
Chains: A, B
Length: 337 amino acids
Theoretical weight: 37.59 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Transaldolase/Fructose-6-phosphate aldolase
Structure domains: Aldolase class I
Length: 337 amino acids
Theoretical weight: 37.59 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P37837 (Residues: 1-337; Coverage: 100%)
Sequence domains: Transaldolase/Fructose-6-phosphate aldolase
Structure domains: Aldolase class I
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
MAX II BEAMLINE I711
Spacegroup:
P21
Expression system: Escherichia coli
