› 1tcd

X-ray diffraction
1.83Å resolution

Function and Biology Details

Reaction catalysed: 
D-glyceraldehyde 3-phosphate = glycerone phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156485 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase, glycosomal Chains: A, B
Molecule details ›
Chains: A, B
Length: 249 amino acids
Theoretical weight: 27.16 KDa
Source organism: Trypanosoma cruzi
Expression system: Escherichia coli
UniProt:
  • Canonical: P52270 (Residues: 3-251; Coverage: 99%)
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MACSCIENCE
Spacegroup: P212121
Unit cell:
a: 43.71Å b: 77.65Å c: 149.54Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.191 0.258
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Glycolysis as a target for the design of new anti-trypanosome drugs.
Verlinde et al. (2001)
1 more

16 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
15 more