› 3mos

X-ray diffraction
1.75Å resolution

The structure of human Transketolase

Released:
DOI: 10.2210/pdb3mos/pdb
PDB entry 3mos coloured by chain, front view.
PDB entry 3mos coloured by chain, side view.
PDB entry 3mos coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The crystal structure of human transketolase and new insights into its mode of action.
Mitschke L, Parthier C, Schröder-Tittmann K, Coy J, Lüdtke S, Tittmann K
J Biol Chem 285 31559-70 (2010)
PMID: 20667822

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 analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151464 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transketolase Chain: A
Molecule details ›
Chain: A
Length: 616 amino acids
Theoretical weight: 67.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P29401 (Residues: 3-618; Coverage: 99%)
Gene name: TKT
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand TPP 1 x TPP
3 bound ligands:
Ligand CA 1 x CA
Ligand EDO 10 x EDO
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: C2
Unit cell:
a: 113.63Å b: 85.33Å c: 72.74Å
α: 90° β: 125.69° γ: 90°
R-values:
R R work R free
0.164 0.162 0.206
Expression system: Escherichia coli

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Citations

6 review citations

Thiamin diphosphate-dependent enzymes: from enzymology to metabolic regulation, drug design and disease models.
Bunik et al. (2013)
5 more

14 mentions without citation

Mechanistic aspects of carotenoid biosynthesis.
Moise et al. (2014)
13 more