CAR T cell targeting T‐cell receptor β‐chain constant domains 1 (TRBC1) of malignant T cells has been developed using JOVI.1 monoclonal antibody as a template However, the mode of antibody binding is not clear. To explore, the researchers from Prince of Songkla University investigated the molecular interaction between JOVI.1 antibody and TRBC1 by using computational methods and molecular docking. The TRBC protein crystal structures (TRBC1 and TRBC2) as well as the sequences of JOVI.1 CDR were chosen as the starting materials. TRBC1 and TRBC2 epitopes were predicted, and molecular dynamic (MD) simulation was used to visualize the protein dynamic behavior. Epitope prediction suggested that the N3K4 region of TRBC1 may be a key to distinguish TRBC1 from TCBC2. MD simulation showed the major different surface conformation in this area between two TRBCs. The JOVI.1‐TRBC1 structures with three binding modes demonstrated JOVI.1 interacted TRBC1 at N3K4 residues, with the predicted dissociation constant (Kd) ranging from 1.5 × 10⁸ to 1.1 × 10¹⁰ M. The analysis demonstrated JOVI.1 needed D1 residues of TRBC1 for the interaction formation to N3K4 in all binding modes. This data was useful for JOVI.1 redesign to improve the PTCL‐targeting CAR T cell.