Journal of Chemistry

Research Article

Molecular Design and In-Silico Analysis of Trisubstituted Benzimidazole Derivatives as Ftsz Inhibitor

Table 3

Binding energy hydrogen bonding, bond length, other interaction, and RMSD value of ligands.
CodeBinding energy (kcal/mol)Hydrogen bondingBond length (Å)Other interactionsRMSD value
A1−8.0THR106, PHE180, ASP 1842.02, 2.51, 2.09/2.10Π-donor H-bond1.848
A2−9.4THR106, PHE180, ASP 1842.13, 2.66, 1.93Π-donor H-bond2.273 [46]
A3−9.7THR106, PHE180, ASP 1842.16, 2.54, 1.97Π-donor H-bond2.402 [47]
A4−9.4THR106, PHE180, ASP 1842.03, 2.67/2.97, 2.09/2.27Π-donor H-bond, Π-cation1.724
A5−9.5THR106, PHE180, ASP 1842.11, 2.61, 1.94Π-donor H-bond1.560
A6−9.1THR106, PHE180, ASP 1842.12, 2.61, 1.96Π-donor H-bond, Π-σ bond1.643
A7−9.3THR106, PHE180, ARG181, ASP 1842.19, 2.64, 2.85, 1.95Π-donor H-bond2.155 [46]
A8−9.3THR106, PHE180, ARG181, ASP 1842.10, 2.61, 3.05, 1.95Π-donor H-bond1.524
A9−9.6THR106, PHE180, ASP 1842.07, 2.50, 1.96/2.25/3.37Π-donor H-bond1.639
A10−9.7THR106, PHE180, ASP 1841.99, 2.47, 2.03/2.06Π-donor H-bond, C-H-bond1.488
A11−9.7THR106, PHE180, ASP 1841.99, 2.59, 2.02/2.06Π-donor H-bond, C-H-bond2.205 [48]
A12−9.3GLY107, PHE180, ASP 1842.20, 2.96, 1.88/2.07Π-donor H-bond, Π-σ bond1.514
A13−9.2GLY107, PHE180, ASP 1842.24, 2.95, 1.87/1.96Π-donor H-bond, Π-σ bond1.643
A14−9.3GLY107, PHE180, ASP 1842.19, 2.95, 1.86/2.05Π-donor H-bond, Π-σ bond1.927
A15−10.2GLY107, PHE180, ASP 1842.26, 2.57, 1.93/2.29Π-donor H-bond, Π-σ bond2.016 [49]
A16−9.6THR106, PHE180, ASP 1841.97, 2.48/2.08, 3.07/1.99Π-donor H-bond1.702
A17−9.7GLY105, THR106, PHE180, ASP 1842.49, 2.02, 2.49 2.02/2.25/3.30Π-donor H-bond2.042 [47]
A18−9.7THR106, PHE180, ASP 1842.05, 2.49, 1.99/2.25/3.26Π-donor H-bond1.562
A19−9.8THR106, PHE180, ASP 1842.10, 2.53, 1.91/2.19Π-donor H-bond1.797
A20−9.8THR106, PHE180, ASP 1841.96, 2.53/3.02, 2.03/2.01Π-donor H-bond1.529
A21−7.7ALA70, THR106, ARG140, GLU1362.42, 2.11/2.34, 3.08, 2.39C-H-bond, halogen1.710