Drug Discovery Against Mtb InhA

InhA is a therapeutic target in Mycobacterium tuberculosis. The S94A mutation and its effect on isoniazid interactions were examined as part of understanding the target.

Comparing candidate inhibitors requires consistent structural evidence — docking affinity, interaction distances and drug-likeness parameters, rather than a single metric.

Protein and ligand information was retrieved from PDB and PubChem; the target structure was prepared and the active site identified.

Molecular docking was performed and protein–ligand interactions analyzed using PyMOL.

Isoniazid, pyridomycin and NITD-916 were compared using docking affinity, interaction distances and SwissADME drug-likeness parameters.

Candidates were prioritized according to the project’s reported criteria.

• Data retrieval — target and ligand structures from PDB and PubChem.
• Preparation — target structure prepared and active site identified.
• Docking — molecular docking performed with AutoDock.
• Interaction analysis — protein–ligand interactions analyzed with PyMOL.
• Drug-likeness — SwissADME parameters across isoniazid, pyridomycin and NITD-916.
• Prioritisation — candidates ranked by the project’s reported criteria.

• Investigated InhA as a therapeutic target and examined the S94A mutation and its effect on isoniazid interactions.
• Retrieved protein and ligand information from PDB and PubChem, prepared the target and identified the active site.
• Performed molecular docking, then analyzed protein–ligand interactions using PyMOL, and compared the candidates on affinity, interaction distances and drug-likeness.

Results and detailed analysis available in the project repository.

• A candidate ranking depends on combining docking affinity, interaction distances and drug-likeness rather than any single score.
• Consistent structural preparation matters before any docking comparison is meaningful.
• Standard public resources — PDB, PubChem, SwissADME — keep a docking study reproducible and shareable.