X-ray diffraction
3.37Å resolution

X-ray structure of Trypanothione Reductase from Leishmania infantum in complex with 2-(diethylamino)ethyl 4-((3-(4-nitrophenyl)-3-oxopropyl)amino)benzoate


Function and Biology Details

Reaction catalysed:
Trypanothione + NADP(+) = trypanothione disulfide + NADPH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Trypanothione reductase Chain: A
Molecule details ›
Chain: A
Length: 488 amino acids
Theoretical weight: 52.77 KDa
Source organism: Leishmania infantum
Expression system: Escherichia coli
  • Canonical: A4HSF7 (Residues: 1-488; Coverage: 99%)
Gene names: LINJ_05_0350, TRYR
Sequence domains:
Structure domains:

Ligands and Environments

Cofactor: Ligand FAD 1 x FAD
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P41212
Unit cell:
a: 103.33Å b: 103.33Å c: 191.55Å
α: 90° β: 90° γ: 90°
R R work R free
0.206 0.203 0.265
Expression system: Escherichia coli