Salgado-Moran, G.Ramirez-Tagle, R.Glossman-Mitnik, D.Ruiz-Nieto, S.Kishore-Deb, P.Bunste, M.Lobos-Gonzalez, F.2023-05-152023-05-152013Journal of Chemistry, 2013, Article number 6012702090-9071https://repositorio.unab.cl/xmlui/handle/ria/49628Indexación: Scopus.The binding of ethambutol to the C-terminal domain of the arabinosyltransferase from Mycobacterium tuberculosis was studied. The analysis was performed using an in silico approach in order to find out, by docking calculations and energy descriptors, the conformer of Ethambutol that forms the most stable complex with the C-terminal domain of arabinosyltransferase. The complex shows that location of the Ethambutol coincides with the cocrystallization ligand position and that amino acid residues ASH1051, ASN740, ASP1052, and ARG1055 should be critical in the binding of Ethambutol to C-terminal domain EmbC.enContainer ClosuresIntegrity TestsPackagingDocking studies of binding of ethambutol to the C-terminal domain of the arabinosyltransferase from mycobacterium tuberculosisArtÃculoAttribution 3.0 Unported (CC BY 3.0)10.1155/2013/601270