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TitleIdentification and binding mode of a novel Leishmania Trypanothione reductase inhibitor from high throughput screening.
Journal, issue, pagesPlos Negl Trop Dis, Vol. 12, Page e0006969-e0006969, Year 2018
Publish dateOct 17, 2017 (structure data deposition date)
AuthorsTurcano, L. / Torrente, E. / Missineo, A. / Andreini, M. / Gramiccia, M. / Di Muccio, T. / Genovese, I. / Fiorillo, A. / Harper, S. / Bresciani, A. ...Turcano, L. / Torrente, E. / Missineo, A. / Andreini, M. / Gramiccia, M. / Di Muccio, T. / Genovese, I. / Fiorillo, A. / Harper, S. / Bresciani, A. / Colotti, G. / Ilari, A.
External linksPlos Negl Trop Dis / PubMed:30475811
MethodsX-ray diffraction
Resolution3.37 Å
Structure data

PDB-6er5:
X-ray structure of Trypanothione Reductase from Leishmania infantum in complex with 2-(diethylamino)ethyl 4-((3-(4-nitrophenyl)-3-oxopropyl)amino)benzoate
Method: X-RAY DIFFRACTION / Resolution: 3.37 Å

Chemicals

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

ChemComp-BVN:
2-(diethylamino)ethyl 4-((3-(4-nitrophenyl)-3-oxopropyl)amino)benzoate

ChemComp-SO4:
SULFATE ION

Source
  • leishmania infantum (eukaryote)
KeywordsOXIDOREDUCTASE / trypanothione / trypanothione reductase / Leishmania Infantum trypanothione reductase inhibitors.

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