› 2r8p

X-ray diffraction
1.65Å 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 T6F 2 x T6F
2 bound ligands:
Ligand CA 2 x CA
Ligand EDO 9 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: 90.214Å b: 101.863Å c: 133.345Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.156 0.156 0.18
Expression system: Escherichia coli

Quick links

Citations

8 review citations

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

2 mentions without citation

A preliminary X-ray study of transketolase from Burkholderia pseudomallei.
Kim et al. (2012)
1 more