› 2r5n

X-ray diffraction
1.6Å 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-541465 (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
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 TPP 2 x TPP
4 bound ligands:
Ligand R5P 1 x R5P
Ligand CA 2 x CA
Ligand EDO 16 x EDO
Ligand RP5 2 x RP5
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P212121
Unit cell:
a: 89.969Å b: 101.738Å c: 132.859Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.163 0.196
Expression system: Escherichia coli

Quick links

Citations

8 review citations

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

2 mentions without citation

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