Fig 1.
Cartoon representation of envelope protein showing chain A, chain B, Domains, and βOG.
Fig 2.
Binding interactions between the first docked βOG (grey), sourced from PDB, and the re-docked βOG (yellow) ensure an RMSD of less than 2 Å.
Table 1.
Ligands with its binding affinity.
Table 2.
Key amino acids and various interaction types among the top 3 candidates.
Fig 3.
Two-dimensional projection of the protein-ligand interaction.
(a) FLA1 (b) FLA2 (c) FLA3 (d) Native ligand (e) Reference ligand.
Fig 4.
(a) the protein backbone relative to the ligand (b) the protein backbone related to the protein backbone, c) The RMSF curves of the protein’s α-carbon atoms, (d) The protein’s Rg curves, (e) The SASA of the protein, and (f) The count of hydrogen bonds that bind ligands to proteins in various complexes derived from 100 ns MDS trajectories.
Fig 5.
RDFs of highly interacting atom pairs among the ligand and protein residues that form H-bonds with each other in,
(a) FLA1, (b) FLA2, (c) FLA3, (d) Native ligand, and (e) Reference ligand.
Fig 6.
Images capturing the ligand’s positioning at the orthosteric site during MDS.
Orientation and location of ligands (shown in ball and stick model) to be monitored at various times.
Table 3.
The components of binding free energy change (ΔGBFE: mean with standard deviation) for complexes.