› 2h2q

X-ray diffraction
2.4Å resolution

Function and Biology Details

Reactions catalysed: 
5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH
5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173282 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional dihydrofolate reductase-thymidylate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 521 amino acids
Theoretical weight: 58.9 KDa
Source organism: Trypanosoma cruzi
Expression system: Escherichia coli
UniProt:
  • Canonical: Q27793 (Residues: 1-521; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAP 2 x NAP
1 bound ligand:
Ligand DU 2 x DU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: C2221
Unit cell:
a: 88.681Å b: 137.25Å c: 189.27Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.206 0.241
Expression system: Escherichia coli

Quick links

Citations

4 review citations

New, improved treatments for Chagas disease: from the R&D pipeline to the patients.
Ribeiro et al. (2009)
3 more

5 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)
4 more