This study presents near-atomic-resolution structures of LRRK2 bound to type I (LRRK2-IN-1 and GNE-7915) and type II (rebastinib, ponatinib, and GZD-824) kinase inhibitors, revealing the structural basis of LRRK2 inhibition and conformational plasticity of the kinase domain through molecular dynamics (MD) simulations. Type I and II inhibitors bind to LRRK2 in active-like and inactive conformations, respectively, providing insights into general structural features associated with LRRK2 activation. The study provides atomic details of LRRK2-inhibitor interactions and a framework for understanding LRRK2 activation and rational drug design. The results highlight the importance of specific interactions between LRRK2 and inhibitors, such as the polar interactions involving A1950, D2017, and E1920, and the unique helical structure of the activation loop, which "melts" upon activation or inhibitor binding. Additionally, the MD simulations reveal metastable states in the apo KIN domain, suggesting potential targets for computational drug discovery. This work advances the understanding of LRRK2 inhibition and offers a foundation for developing more effective LRRK2-specific inhibitors.This study presents near-atomic-resolution structures of LRRK2 bound to type I (LRRK2-IN-1 and GNE-7915) and type II (rebastinib, ponatinib, and GZD-824) kinase inhibitors, revealing the structural basis of LRRK2 inhibition and conformational plasticity of the kinase domain through molecular dynamics (MD) simulations. Type I and II inhibitors bind to LRRK2 in active-like and inactive conformations, respectively, providing insights into general structural features associated with LRRK2 activation. The study provides atomic details of LRRK2-inhibitor interactions and a framework for understanding LRRK2 activation and rational drug design. The results highlight the importance of specific interactions between LRRK2 and inhibitors, such as the polar interactions involving A1950, D2017, and E1920, and the unique helical structure of the activation loop, which "melts" upon activation or inhibitor binding. Additionally, the MD simulations reveal metastable states in the apo KIN domain, suggesting potential targets for computational drug discovery. This work advances the understanding of LRRK2 inhibition and offers a foundation for developing more effective LRRK2-specific inhibitors.