Fig. 6

In silico modeling reveals preferential Kaempferol binding to the nucleotide-binding domain of GRP75. a Table depicting Vina scores, and cavity information of the docking simulation pose for GRP75 nucleotide-binding domain (NBD) and KMP. b The structure of KMP was uploaded to CB-Dock for analysis of the docking potential with GRP75. The crystal structure of the human GRP75 nucleotide-binding domain (PDB ID: 6NHK), the active site is colored white (carbon), red (oxygen), blue (nitrogen), and yellow (sulphur). The crystal pose of the ligand KMP in the cavity sized 3793 is colored white (hydrogen), grey (carbon), and red (oxygen). c Table depicting Vina scores, and cavity information of the docking simulation pose for GRP75 nucleotide-binding domain (NBD) and 17-AAG. d The crystal structure of the human GRP75 nucleotide-binding domain (PDB ID: 6NHK), the active site is colored white (carbon), red (oxygen), blue (nitrogen), and yellow (sulphur). The crystal pose of the ligand 17-AAG in the cavity sized 3793 is colored white (hydrogen), grey (carbon), and red (oxygen). Note the comparatively lower Vina score for 17-AAG binding to GRP75-NBD compared to that of KMP within the same pocket, suggesting a stronger fit of KMP in the NBD domain of GRP75. e Venn diagram depicting the number of overlapping human proteins that are targeted by both KMP and 17-AAG. The PharmMapper database was used to predict the targets of Kmp and 17-AAG. This mapping predicted a large overlap of targets shared (cut-off z-score: 0.5) by the two compounds, including HSP90A. Both ligands did not target GRP75. See Suppl. Table 1 for the complete list of overlapping targets