D with B: Lys 352 with the S9 sheet. Therefore, we discovered that the ligand interacted predominantly together with the amino acids from the secondary components on the T7 loop, H8 helix, and S9 sheet of CBS. The kinds of non-covalent interactions with these amino acids, which includes the formation of hydrogen, hydrophobic, ionic interactions, and the formation of water bridges, too as the contribution of every interaction form for the all round interaction using a unique amino acid, are shown within the Figures 8A and 9. The time-dependent total number of contacts involving the ligand and protein and the number of contacts among the ligand and distinct amino acids are shown in Figure 8B.Molecules 2022, 27, x FOR PEER REVIEW11 ofMolecules 2022, 27,trajectory evaluation showed the low RMSD values on the ligands and proteins (Figure 7), which indicates the absence of massive fluctuations throughout the whole time of molecular dynamics.11 ofMolecules 2022, 27, x FOR PEER Critique Figure 7. Change in RMSD (root means square deviation) for ligand (pink12 of 20 Figure 7. Change in RMSD (root indicates square deviation) for ligand (pink colour) and for C atoms colour) and for of tubulin dimer (blue color) in the course of during unbiased of unbiased molecular dynamic simulation. tubulin dimer (blue colour) one hundred ns of one hundred ns molecular dynamic simulation.C atoms ofOver the one hundred nanoseconds of molecular dynamics, EAPC-67 predominantly formed the non-covalent contacts together with the following amino acids B: Leu 248, B: Asn 249, B: Ala 250, B: Asp 251 with the T7 loop, with B: Lys 254, B: Leu 255 of the H8 helix and with B: Lys 352 of the S9 sheet. For that reason, we identified that the ligand interacted predominantly with the amino acids of the secondary elements with the T7 loop, H8 helix, and S9 sheet of CBS. The varieties of non-covalent interactions with these amino acids, including the formation of hydrogen, hydrophobic, ionic interactions, and the formation of water bridges, also as the contribution of every interaction type towards the all round interaction with a specific amino acid, are shown in the Figures 8A and 9. The time-dependent total quantity of contacts amongst the ligand and protein along with the variety of contacts in between the ligand and specific amino acids are shown in Figure 8B.Figure eight. (A) (A) Protein-ligand fraction interaction diagram among EAPC-67 and tubulin.MNS Purity & Documentation H-bonds, Figure eight.Lithium chloride hydrate Protein-ligand fraction interaction diagram between EAPC-67 and tubulin.PMID:25818744 H-bonds, ionic, hydrophobic interactions, and water bridges are shown in green, red, purple, and blue, reionic, hydrophobic interactions, and amino bridges are shown in web page in the course of the spectively. (B) Contact points of EAPC-67 andwater acids of colchicine binding green, red, purple, and blue, respecwhole simulation trajectory. The topEAPC-67 and total number of protein-ligand contacts over tively. (B) Contact points of panel shows the amino acids of colchicine binding site through the whole 100 ns.simulation trajectory. The best panel shows the total quantity of protein-ligand contacts more than 100 ns.Molecules 2022, 27, x FOR PEER Assessment Molecules 2022, 27,13 of 20 12 ofFigure 9. 2D plot of ligand-protein fraction interaction diagram amongst EAPC-67 and tubulin Figure 9. 2D plot of ligand-protein amino interaction kind of between EAPC-67 and tubulin more than 100 nanoseconds MD with labeled key fractionacids. Eachdiagram non-covalent interaction is highlightedover one hundred nanoseconds MD with labeled crucial amino acids. Each and every variety of non-covalent interaction is within the correspond.