› 2r8o

X-ray diffraction
1.47Å 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-150967 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transketolase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 669 amino acids
Theoretical weight: 73.12 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P27302 (Residues: 1-663; Coverage: 100%)
Gene names: JW5478, b2935, tkt, tktA
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand T5X 2 x T5X
2 bound ligands:
Ligand CA 2 x CA
Ligand EDO 11 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P212121
Unit cell:
a: 90.138Å b: 101.951Å c: 133.258Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.15 0.15 0.164
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Stabilizing biocatalysts.
Bommarius et al. (2013)
7 more

5 mentions without citation

Structure and function of the transketolase from Mycobacterium tuberculosis and comparison with the human enzyme.
Fullam et al. (2012)
4 more