Introduction: Numerous malignancies, ranging from breast cancer, non-small cell lung cancer and chronic myeloid leukemia, are driven by aberrant tyrosine kinase signaling. Given the well-documented toxicity of current chemotherapeutic medicines, there is a great need and demand for the discovery of novel drugs that are either toxic-free or having low toxicity, while effectively targeting and inhibiting the growth of tumor cells. This work describes the in-silico examination of substances from the drug bank as potential EGFR inhibitors. Methods: Firstly, the drug bank was screened using the pharmacophore technique to select ligands. Erlotinib (DB00530) was used as a reference compound. The selected ligands were screened using ADMET analysis and the hit compounds were subsequently subjected to docking studies. The lead compound from docking studies was subjected to Density Functional Theory (DFT) and Molecular Dynamics (MD) simulation studies. Results: Using the pharmacophore technique, 23 compounds were identified through virtual drug bank screening. One hit molecule from ADMET prediction was the subject for docking study. According to the findings, DB03365 molecule fits to the EGFR active site by forming several hydrogen bond interactions with amino acids. DFT analysis revealed high reactivity of DB03365 compound within the binding pocket of the target protein, as indicated by ELUMO, EHOMO and band energy gap values. Furthermore, MD simulations for 100 ns revealed that the ligand interactions with the residues of EGFR protein were part of the essential residues for structural stability and functionality. Conclusion: DB03365 was found to be highly selective for EGFR, suggesting its potential as a therapeutic agent. However, further studies are warranted to thoroughly explore the therapeutic potentials of DB03365. [ABSTRACT FROM AUTHOR]