In this study, the three-dimensional (3-D) structures of lung cancer cell line proteins (p38, epidermal growth factor (EGFR) and B-cell lymphoma 2 (Bcl-2), were developed and their binding affinities with coumaric acid, anthraquinone, gingerol, tanshinone, baicalein and wogonin through local docking were evaluated. Firstly, Swiss model was used to generate p38, EGFR and Bcl-2. After that, they were viewed by the PyMol software. Next, Expasy’s ProtParam Proteomics server was used to determine the physical and chemical parameters of the protein models. Moreover, the protein models validated using PROCHECK, ProQ, ERRAT and Verify 3D programs. Finally, the protein models were docked with coumaric acid, anthraquinone, gingerol, tanshinone, baicalein and wogonin by using BSP-Slim server. After the validation and verification process, all the protein models were stable. The p38 showed binding energy with coumaric acid, anthraquinone, gingerol, tanshinone, baicalein and wogonin at -6.72, -5.97, -6.98, -6.52, -7.70 and -7.21 kcal/mol respectively. Besides that, the EGFR showed binding energy of coumaric acid, anthraquinone, gingerol, tanshinone, baicalein and wogonin at -7.38, -6.53, -7.41, -7.05, -6.69 and -6.84 kcal/mol respectively. Moreover, the Bcl-2 showed binding energy of coumaric acid, anthraquinone, gingerol, tanshinone, baicalein and wogonin at -6.74, -5.97, -6.06, -5.41, -6.54 and -5.13 kcal/mol respectively. The p38 had the strongest bond with wogonin; the EGFR protein had the strongest interaction with gingerol; while Bcl-2 had the strongest binding affinity with coumaric acid.