PDBe 1f05

X-ray diffraction
2.45Å resolution

CRYSTAL STRUCTURE OF HUMAN TRANSALDOLASE

Released:
Source organism: Homo sapiens
Primary publication:
The three-dimensional structure of human transaldolase.
FEBS Lett. 475 205-8 (2000)
PMID: 10869557

Function and Biology Details

Reaction catalysed:
Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transaldolase Chains: A, B
Molecule details ›
Chains: A, B
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%)
Gene names: TAL, TALDO, TALDO1, TALDOR
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

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P21
Unit cell:
a: 45.57Å b: 113.57Å c: 69.19Å
α: 90° β: 101.37° γ: 90°
R-values:
R R work R free
0.254 0.225 0.258
Expression system: Escherichia coli