2.8.9. Molecular Docking

The molecular docking analysis was performed by using InstaDock v1.0 software, New Delhi, India (https://hassanlab.org, accessed on 1 April 2022), ChemBioDraw Ultra 14.0, inhouse python script and Discovery Studio as mentioned in the experimental section [65–69]. It included the fundamental orientations between the receptor and the ligands (plant extract phytoconstituents). The 10 shortlisted proteins were used for molecular docking in order to explain how these proteins interact with the phytoconstituents identified in the ethyl acetate aerial part of *A. aspera* and flower ash extract of *C. gigantea*. The high negative docking score (binding free energy, kcal/mol) indicated that their binding was steady. In Table S7, the comparative analysis of docking results on the multitarget proteins is provided. The docking scores are shown in Figure 7. The 2D structure of the phytoconstituents is provided in Figure S3. The selected top hit phytoconstituents had binding free energies ranging from −7.5 to −10.6 kcal/mol, and the correspomding proteins were chosen for further studies. *β*-amyrin (PubChem CID: 225689) was found to have higher binding free energies against *Rv1636*, *Rv1566*, *Rv2549c*, and *Rv1495* proteins. The 3D crystal structures of VDA proteins, showing different conformational changes, were identified and structural analysis was carried out using a PyMOL visualizer (Figure 8).
