Figure 1. Molecular docking analysis shows Ginsenoside Rb1 binding with GABAA receptor. (A) Original 2D image of Rb1. (B) Modified 3D image of Rb1. (C) Overall map of Rb1 interaction with GABAARα1. (D) Interaction between Rb1 with the TMD of GABAARα1 receptor. Note that when Rb1 (indicted by green stick) was docked in the TMD of GABAARα1, two hydrogen bonds formed with Ile239 and Trp246 sites (indicated by red dotted line). Besides, Rb1 also formed a hydrophobic interaction with multiple hydrophobic amino acids or hydrophobic parts of polar amino acids in the TMD domain of GABAARα1 (Ile235, Val238, Ile239, Val243, Trp246, Phe298, Ile302, Ala305, Thr306, Tyr309, Phe310, Ary397, Pro401, Leu402, Phe404) (indicated by blue stick).