Our work examines the effect of molecular motor binding reactions on intracellular transportation. Motor proteins (namely kinesin and dynein) carry cargo along microtubule at rates faster than diffusion would allow. However, molecular motors are known to have low processivity, thus spending a significant amount of time freely diffusing with their cargo. We therefore seek to model this system to connect aspects of this complex dynamic to its efficiency. This model is examined as a Partial Differential Equation, a probability density function, and a Monte Carlo simulation. Emphasis is placed on binding reactions needed to create active crosslinks between cargo and the microtubule. We have shown that when cargo have multiple motor binding sites, motors with low processivity optimize microtubule flux by increasing cargo binding while maintaining at least one active crosslink. Our work highlights the benefit of current molecular motor transport and presents an alternative process for engineering motors that could augment processes such as protein synthesis and modification, cell signaling, and cell repairing.