› 1gpu

X-ray diffraction
1.86Å resolution

Function and Biology Details

Reaction catalysed: 
Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149906 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transketolase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 680 amino acids
Theoretical weight: 73.89 KDa
Source organism: Saccharomyces cerevisiae
UniProt:
  • Canonical: P23254 (Residues: 1-680; Coverage: 100%)
Gene names: TKL1, YP9499.29C, YPR074C
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand THD 2 x THD
1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P212121
Unit cell:
a: 74.3Å b: 113.2Å c: 159.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.198 0.225

Quick links

Citations

3 review citations

Advances in kinetic protein crystallography.
Bourgeois et al. (2005)
2 more

5 mentions without citation

Snapshot of a key intermediate in enzymatic thiamin catalysis: crystal structure of the alpha-carbanion of (alpha,beta-dihydroxyethyl)-thiamin diphosphate in the active site of transketolase from Saccharomyces cerevisiae.
Fiedler et al. (2002)
4 more