› 1tka

X-ray diffraction
2.7Å resolution

SPECIFICITY OF COENZYME BINDING IN THIAMIN DIPHOSPHATE DEPENDENT ENZYMES: CRYSTAL STRUCTURES OF YEAST TRANSKETOLASE IN COMPLEX WITH ANALOGS OF THIAMIN DIPHOSPHATE

Released:
DOI: 10.2210/pdb1tka/pdb
PDB entry 1tka coloured by chain, front view.
PDB entry 1tka coloured by chain, side view.
PDB entry 1tka coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Specificity of coenzyme binding in thiamin diphosphate-dependent enzymes. Crystal structures of yeast transketolase in complex with analogs of thiamin diphosphate.
König S, Schellenberger A, Neef H, Schneider G
J Biol Chem 269 10879-82 (1994)
PMID: 8144674

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: 678 amino acids
Theoretical weight: 73.66 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Not provided
UniProt:
  • Canonical: P23254 (Residues: 3-680; Coverage: 100%)
Gene names: TKL1, YP9499.29C, YPR074C
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand N3T 2 x N3T
1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 76.3Å b: 113.3Å c: 160.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.158 0.158 not available
Expression system: Not provided

Quick links

Citations

4 review citations

Properties and functions of the thiamin diphosphate dependent enzyme transketolase.
Schenk et al. (1998)
3 more

3 mentions without citation

Molecular-docking study of malaria drug target enzyme transketolase in Plasmodium falciparum 3D7 portends the novel approach to its treatment.
Hasan et al. (2015)
2 more