In the quest for effective lung cancer treatments, the potential of 3,6‐diaminoacridine‐9‐carbonitrile (DAC) has emerged as a game changer. While DAC's efficacy against glioblastoma is well documented, its role in combating lung cancer has remained largely untapped. This study focuses on CTX‐1, exploring its interaction with the pivotal EGFR‐TKD protein, a crucial target in lung cancer therapeutics. A meticulous molecular docking analysis revealed that CTX‐1 exhibits a noteworthy binding affinity of −7.9 kcal/mol, challenging Erlotinib, a conventional lung cancer medication, which displayed a binding affinity of −7.3 kcal/mol. For a deeper understanding of CTX‐1's molecular mechanics, this study employed rigorous 100‐ns molecular dynamics simulations, demonstrating CTX‐1's remarkable stability in comparison with erlotinib. The Molecular Mechanics Poisson–Boltzmann Surface Area (MM‐PBSA) method further corroborated these results, with CTX‐1 showing a free binding energy of −105.976 ± 1.916 kJ/mol. The true prowess of CTX‐1 was tested against diverse lung cancer cell lines, including A549, Hop‐62 and H‐1299. CTX‐1 not only significantly outperformed erlotinib in anticancer activity but also exhibited a spectrum of therapeutic effects. It effectively diminished cancer cell viability, induced DNA damage, halted cell cycle progression, generated reactive oxygen species (ROS), impaired mitochondrial transmembrane potential, instigated apoptosis and successfully inhibited EGFR‐TKD. This study not only underscores the potential of CTX‐1 a formidable contender in lung cancer treatment but also marks a paradigm shift in oncological therapeutics, offering new horizons in the fight against this formidable disease.