Aim. To explain the natural resistance of Daucus carota L. to dinitroaniline herbicides. To clarify features of the carrot α-tubulin that may affect formation of the ligand-protein complex based on the structural and electrostatic analysis of the ligand-binding site. Methods. Reconstruction of the spatial structure of α-tubulin from D. carota and Toxoplasma gondii using profile (Swiss-Model) and de-novo (AlphaFold2) modeling. Molecular dynamics (MD) simulations of the built 3D-models in Gromacs. Analysis of the molecular electrostatics with PDB2PQR/APBS tools. Visualization and analysis of molecular structures in PyMOL. Results. It has been shown that along with the typical positive charge of the dinitroaniline-binding pocket, all isotypes of carrot α-tubulin demonstrate negatively charged regions that may cause conflicts with the nitro-groups of the ligands. Also, the MD-stable negatively charged "bridge" between Cys316 and the aryl-fragment of Phe255 was observed in all α-tubulin isotypes. In our opinion, it not only competes with the cyclic fragment of dinitroanilines, but overall prevent the opening of the site pocket in carrot α-tubulin. Conclusions. It was clarified that natural resistance of D. carota to dinitroaniline herbicides may be associated with steric and electrostatic conflicts observed in in all α-tubulin isotypes. In our opinion, it prevents interaction with dinitroaniline compounds at the stage of primary site recognition on the early stages of protein-ligand complex formation.