Molecular docking simulation of catechin and its derivatives on Glucosamine-6-\nPhosphate Synthase (GlmS) has been performed in this research. GlmS inhibition by a\nparticular ligand will suppress the production of bacterial cell wall and significantly reduce the\npopulation of invading bacteria. In this study, catechin derivatives i.e epicatechin, galloatechin\nand epigalloatechin were found to have stronger binding affinities as compared to natural\nligand of GlmS, Fructose-6-Phosphate (F6P). Those three ligands were docked on the same\npocket in GlmS target as F6P, with 70% binding sites similarity. Based on the docking results,\ngallocatechin turns out to be the most potent ligand for anti-bacterial agent with Ã?â?G= -8.00\nkcal/mol. The docking between GlmS and catechin derivatives are characterized by a constant\npresent of a strong hydrogen bond between functional group O3 and Ser-349. This hydrogen\nbond most likely plays a significant role in the docking mechanism and binding modes\nselection. The surprising result is catechin itself exhibited a quite strong binding with GlmS\n(Ã?â?G= -7.80 kcal.mol), but docked on a completely different pocket compared to other ligands.\nThis results suggest that catechin might still have a curing effect but with a completely\ndifferent pathway and mechanism as compared to its derivatives.
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