› 5xps

X-ray diffraction
1.07Å resolution

Crystal Structure of Transketolase in complex with erythrose-4-phosphate from Pichia Stipitis

Released:
DOI: 10.2210/pdb5xps/pdb
PDB entry 5xps coloured by chain, front view.
PDB entry 5xps coloured by chain, side view.
PDB entry 5xps coloured by chain, top view.
Source organism: Scheffersomyces stipitis CBS 6054
Primary publication:
Evidence of Diradicals Involved in the Yeast Transketolase Catalyzed Keto-Transferring Reactions.
Hsu NS, Wang YL, Lin KH, Chang CF, Ke SC, Lyu SY, Hsu LJ, Li YS, Chen SC, Wang KC, Li TL
Chembiochem 19 2395-2402 (2018)
PMID: 30155962

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-152718 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transketolase Chain: A
Molecule details ›
Chain: A
Length: 697 amino acids
Theoretical weight: 75.05 KDa
Source organism: Scheffersomyces stipitis CBS 6054
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: P34736 (Residues: 1-677; Coverage: 100%)
Gene names: PICST_67105, TKT, TKT1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand TPP 1 x TPP
3 bound ligands:
Ligand PEG 4 x PEG
Ligand E4P 1 x E4P
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL15A1
Spacegroup: C2221
Unit cell:
a: 101.149Å b: 185.246Å c: 98.71Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.119 0.119 0.132
Expression system: Escherichia coli K-12

Quick links

Citations

1 citations in other articles

Structural and chemical trapping of flavin-oxide intermediates reveals substrate-directed reaction multiplicity.
Lin et al. (2020)

1 mention without citation

Evidence of Diradicals Involved in the Yeast Transketolase Catalyzed Keto-Transferring Reactions.
Hsu et al. (2018)