Fig 1.
Ramachandran plot for the model of the structure of ERα (PDB: 6CBZ) and human 17β-HSD1 (PDB: 1FDW) proteins generated by PROCHECK.
The red color region denotes residues of the protein in the most favored regions; the brown color denotes residues in the additional allowed regions and the yellow indicates residues in the generously allowed regions.
Fig 2.
Ramachandran plot for the model of the structure of human TOP2A (PDB: 5GWK) and human p73 tetramerization domain (PDB: 2WTT) proteins generated by PROCHECK.
The red color region denotes residues of the protein in the most favored regions; the brown color denotes residues in the additional allowed regions and the yellow indicates residues in the generously allowed regions.
Fig 3.
Z-score for the model of the structure of multiple proteins generated by ProSA web tool.
Fig 4.
Interaction of ERα (PDB: 6CBZ) with Ashwagandhanolide and Withanolide sulfoxide.
Three-dimensional (3D) illustration shows the interaction of ligands with ERα structure and two-dimensional (2D) diagram displays the interactions of the ligand with the specific amino acid residues in the active site of the protein.
Fig 5.
Interaction of human 17β-HSD1 (PDB: 1FDW) with Ashwagandhanolide and Withanolide Sulfoxide.
Three-dimensional (3D) illustration shows the interaction of ligands with human 17β-HSD1 structure and two-dimensional (2D) diagram displays the interactions of the ligand with the specific amino acid residues in the active site of the protein.
Fig 6.
Interaction of human TOP2A (PDB: 5GWK) with Ashwagandhanolide and Withanolide sulfoxide.
Three-dimensional (3D) illustration shows the interaction of ligands with human TOP2A structure and two-dimensional (2D) diagram displays the interactions of the ligand with the specific amino acid residues in the active site of the protein.
Fig 7.
Interaction of human p73 tetramerization domain (PDB: 2WTT) with Ashwagandhanolide and Withanolide Sulfoxide.
Three-dimensional (3D) illustration shows the interaction of ligands with human p73 tetramerization domain structure and two-dimensional (2D) diagram displays the interactions of the ligand with the specific amino acid residues in the active site of the protein.
Table 1.
Molecular docking results of phytochemicals isolated from W. somnifera against four different proteins expressed during breast cancer.
Fig 8.
Analysis of RMSD (A), Rg (B), SASA (C) and Hydrogen (D) graphs of TOP2A (PDB: 5GWK) in complex with Ashwagandhanolide (Back color indicating protein alone and Red indicating protein-ligand complex).
Table 2.
Chemical structural properties of Ashwagandhanolide.
Table 3.
Predicted ADMET properties of Ashwagandhanolide.
Table 4.
Global Reactivity Descriptors of the Ashwagandhanolide molecular system.
Fig 9.
Graphical representation of the dual descriptor DD of Ashwangandhanolide.
Top: DD > 0, Bottom: DD < 0.