Entry Database : PDB / ID : 6er5 Structure visualization Downloads & linksTitle X-ray structure of Trypanothione Reductase from Leishmania infantum in complex with 2-(diethylamino)ethyl 4-((3-(4-nitrophenyl)-3-oxopropyl)amino)benzoate ComponentsTrypanothione reductase Details Keywords OXIDOREDUCTASE / trypanothione / trypanothione reductase / Leishmania Infantum trypanothione reductase inhibitors.Function / homology Function and homology informationFunction Domain/homology Component
trypanothione-disulfide reductase / trypanothione-disulfide reductase (NADPH) activity / glutathione-disulfide reductase (NADPH) activity / glutathione metabolic process / cell redox homeostasis / flavin adenine dinucleotide binding / cellular response to oxidative stress / mitochondrion / cytosol Similarity search - Function Trypanothione reductase / : / Pyridine nucleotide-disulphide oxidoreductase, class I / FAD/NAD-linked reductase, C-terminal dimerisation domain / Pyridine nucleotide-disulphide oxidoreductase, class I, active site / Pyridine nucleotide-disulphide oxidoreductases class-I active site. / Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain / Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain / FAD/NAD-linked reductase, dimerisation domain superfamily / FAD/NAD(P)-binding domain ... Trypanothione reductase / : / Pyridine nucleotide-disulphide oxidoreductase, class I / FAD/NAD-linked reductase, C-terminal dimerisation domain / Pyridine nucleotide-disulphide oxidoreductase, class I, active site / Pyridine nucleotide-disulphide oxidoreductases class-I active site. / Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain / Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain / FAD/NAD-linked reductase, dimerisation domain superfamily / FAD/NAD(P)-binding domain / Pyridine nucleotide-disulphide oxidoreductase / Enolase-like; domain 1 / FAD/NAD(P)-binding domain / FAD/NAD(P)-binding domain / 3-Layer(bba) Sandwich / FAD/NAD(P)-binding domain superfamily / 2-Layer Sandwich / Alpha Beta Similarity search - Domain/homologyBiological species Leishmania infantum (eukaryote)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 3.37 Å DetailsAuthors Ilari, A. / Fiorillo, A. Funding support Italy, 1items Details Hide detailsOrganization Grant number Country CNCCS Italy
CitationJournal : Plos Negl Trop Dis / Year : 2018Title : Identification and binding mode of a novel Leishmania Trypanothione reductase inhibitor from high throughput screening.Authors : 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. History Deposition Oct 17, 2017 Deposition site : PDBE / Processing site : PDBERevision 1.0 Oct 31, 2018 Provider : repository / Type : Initial releaseRevision 1.1 Jun 12, 2019 Group : Data collection / Database references / Category : citation / citation_author / pdbx_database_procItem : _citation.country / _citation.journal_abbrev ... _citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year Revision 2.0 Oct 23, 2019 Group : Data collection / Non-polymer description / Structure summaryCategory : chem_comp / entityItem : _chem_comp.formula / _chem_comp.formula_weight / _entity.formula_weightRevision 2.1 Jan 17, 2024 Group : Data collection / Database references / Refinement descriptionCategory : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession
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