X-ray diffraction
2.05Å resolution

Crystal structure of human Transketolase (TKT)

Source organism: Homo sapiens
Entry authors: Krojer T, Krysztofinska E, Guo K, Pilka E, Kochan G, Chaikuad A, Vollmar M, von Delft F, Bountra C, Arrowsmith CH, Weigelt J, Edwards A, Kavanagh K, Oppermann U, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed:
Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Transketolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 616 amino acids
Theoretical weight: 67.2 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
  • Canonical: P29401 (Residues: 10-620; Coverage: 98%)
Gene name: TKT
Sequence domains:
Structure domains:

Ligands and Environments

Cofactor: Ligand TDP 2 x TDP
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: P61
Unit cell:
a: 117.23Å b: 117.23Å c: 176.803Å
α: 90° β: 90° γ: 120°
R R work R free
0.201 0.199 0.234
Expression system: Trichoplusia ni