Table 3.
Molecular docking results of the synthesized molecules against 4URO.
| Entry | Dock Score (Kcal/mol) | Interacting Residues | RMSD | RMSF | Lennard-Jones-Short Range: Protein-Ligand (KJ/Mol) | Coulombic-Short Range: Protein-Ligand (KJ/Mol) | Average Radius of gyration | SASA (nm/S2/N) |
|---|---|---|---|---|---|---|---|---|
| 1 | −5.6 | ASN 54, SER 55, ASP 81 by hydrogen bond interactions. ASP 81 by unfavorable acceptor–acceptor interaction. | 0.163 | 0.0674 | −0.0125425 | −0.0346673 | 1.6582 | 114.7077 |
| 2 | −7.2 | ARG 144 by hydrogen bond interaction, GLU 58 by pi-anion interaction, ILE 86, PRO 87, ILE 102 by pi-alkyl interaction. | 0.178 | 0.0817 | −37.9322 | −10.7936 | 1.6672 | 116.9757 |
| 3 | −7.4 | ILE 86, PRO 87, ILE 102 by pi-alkyl interaction, TYR 229 by pi-pi interaction. | 0.229 | 0.884 | −0.335858 | −0.291914 | 1.6818 | 129.0015 |
| 4 | −8.2 | ARG 144, ASN 145 by hydrogen bond interaction, ASP 89, GLU 193 by pi-cation interaction, ARG 84, PRO 87, ILE 86, ILE 102, TYR 227 by pi-pi interaction. | 0.152 | 0.078 | −18.0879 | −0.0175833 | 1.6472 | 128.5847 |
| 5 | −8.4 | TYR 229 by hydrogen bond interaction, GLU 58 by pi-anion interaction, ILE 86, ILE 102, ALA 61 by pi-pi interaction, PHE 204 by pi-pi stacked interaction, ASP 57 by pi-sigma interaction. | 0.111 | 0.0818 | −0.00109673 | 0.00146823 | 1.6449 | 125.8481 |
| 6 | −9.8 | ARG 84 by hydrogen bond interaction, GLU 58 by pi-anion interaction, PHE 204 by pi-pi stacking interaction, ALA 61, ILE 86, ALA 98, ARG 200 by pi-alkyl interaction. | 0.128 | 0.0733 | −10.08751 | 0.431476 | 1.6478 | 124.6634 |
| 7 | −6.2 | GLU 58, ARG 84 by pi-anion interaction, PRO 87 by pi-alkyl interaction. | 0.124 | 0.0655 | −0.00115603 | 0.000529796 | 1.6471 | 115.9002 |
| 8 | −8.6 | ARG 84 by hydrogen bond interaction, PRO 87, ILE 86, ILE 51, VAL 79, PHE 204 by pi-alkyl interaction. | 0.165 | 0.0799 | −0.0349385 | 0.00970908 | 1.6353 | 124.1911 |