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Background  Sterol glycosyltransferases (SGTs) are ubiquitous but one of the most diverse group of enzymes of glycosyltransferases family. Members of this family modulate physical and chemical properties of secondary plant products important for various physiological processes. The role of SGTs has been demonstrated in the biosynthesis of pharmaceutically important molecules of medicinal plants like  Withania somnifera .    Results  Analysis suggested conserved behaviour and high similarity in active sites of  Ws SGTs with other plant GTs. Substrate specificity of  Ws SGTs were analysed through docking performance of  Ws SGTs with different substrates (sterols and withanolides). Best docking results of  Ws SGTL1 in the form of stable enzyme-substrate complex having lowest binding energies were obtained with brassicasterol, transandrosteron and  Ws SGTL4 with solasodine, stigmasterol and 24-methylene cholesterol.    Conclusion  This study reveals topological characters and conserved nature of two SGTs from  W. somnifera  ( Ws SGTs) i.e.  Ws SGTL1 and  Ws SGTL4. However, besides being ubiquitous in nature and with broad substrate specificity, difference between  Ws SGTL1 and  Ws SGTL4 is briefly described by difference in stability (binding energy) of enzyme-substrate complexes through comparative docking.    Electronic supplementary material  The online version of this article (doi:10.1186/s12859-015-0563-7) contains supplementary material, which is available to authorized users.

Comparative interactions of withanolides and sterols with two members of sterol glycosyltransferases from Withania somnifera