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. 2019 Mar 11;9:4073. doi: 10.1038/s41598-019-40626-2

Figure 1.

Figure 1

Andrographolide and tivozanib interacts with common amino acid in the ATP-binding pocket of VEGFR2. (A) 2D binding poses of ligands (i) co-crystal conformation of tivozanib with VEGFR2 (PDB ID: 4ASE), (ii) docked conformation of tivozanib in the kinase domain of VEGFR2, (iii) docked conformation of ATP in the kinase domain of VEGFR2 and (iv) docked conformation of andrographolide in the kinase domain of VEGFR2. All the ligands share common interacting amino acid Asp-1045 and Glu-885. (B) Molecular docking score of ATP, tivozanib, and andrographolide in ATP kinase domain of VEGFR2. (C) Surface model depicts andrographolide in kinase domain of VEGFR2, (i & ii) andrographolide is buried inside the ATP-binding pocket, protein is represented in the surface form, and andrographolide is represented in the stick form. (iii) Binding pocket is magnified for further understanding.