https://orcid.org/0000-0001-7925-2793
Figures & data
Figure 1 In silico study workflow.
Figure 2 The distribution of the 15 mutations according to the function, deleterious or neutral.
Figure 3 (A) The effect of the deleterious mutations on solvent accessibility surface area (SASA) between the wild-type protein (in blue) and the mutanttype protein (in orange). (B) The effect of the deleterious mutations on the flexibility (in orange) and stability (in blue) of the InhA protein.
Figure 4 The three best leads with lowest affinity binding to the wild-type protein and the the mutant models.
Table 1 The essential information about the reference ligand INH-NAD, natural ligand NADH and the Three best ligands including molecular formula, binding affinity score, hydrogen bond CID in PubChem, molecular weight, and toxicity test
Figure 5 Visualization of 3D interactions against InhA protein. (A) Interaction between the reference ligand Inh-NAD and the inhA protein. (B) Interactions between NADH and InhA protein. (C) Interaction between ligand (CID:25176455) and inhA protein. (D) Interaction between ligand (CID:91754233) and InhA protein. (E) Interaction between ligand (CID:101256471) and InhA protein.
Figure 6 The pharmacophore model generated after the flexible alignment of the best three compounds. (A) shows the different features explored in the model structure with the aligned ligands. (B) shows a simplified view of the model without ligands.
