The spatial organization of cellular membranes is crucial for intracellular trafficking processes, where membrane-bound Rab GTPases play a central role. This study explores the formation and dynamics of Rab protein domains, focusing specifically on Rab5 and Rab11, and examines their structural organization and functional roles in endosomal trafficking. Rab proteins act as molecular switches that regulate distinct stages of the endocytic pathway by recruiting various effectors, thereby orchestrating vesicle transport. . Building on previous studies of Rab5/Rab7 domains, we develop a computational model to simulate the formation of Rab5/Rab11 domains. Our simulations demonstrate how, starting from a homogeneous distribution, interactions and reactions among Rab5 and Rab11 proteins lead to the emergence of distinct domains, enhancing our understanding of membrane compartmentalization in cellular trafficking.