The structure and dynamics of water around proteins significantly influence protein-protein interactions. A primitive treatment of the effect of water on protein-protein interactions is to assume that protein hydration is uniform over its surface, which effectively increases the protein excluded volume. The local density and dynamics of hydration waters are, however, sensitive to the local topography and chemical heterogeneity of the protein surface. The spatially heterogeneous distribution of hydration sites alters the configurational complementarity of protein-protein interactions. A description of explicit waters of hydration in protein-protein interactions accounts for this specific hydration, but is computationally prohibitive. Alternatively, continuum models of water, while computationally cost-effective, ignore the role of strongly associated water molecules at the protein-water interface. Motivated by the quasi-chemical view of protein hydration, we identify bound water at defined grid sites around several well-characterized proteins on the basis of local density of water molecules at each grid site. The dynamics of water at the grid sites is characterized in terms of average occupancy and vacancy time distributions. The correspondence between thermodynamic and kinetic perspectives of waters of hydration is obtained as a function of the local environment of the protein. Two distinct kinetic behaviors of bound waters are observed: long periods of occupancy of a site without frequent exchange, or short periods of occupancy of a site with frequent exchanges. In addition, we found that the number of kinetically bound water is about an order less than the number of bound water identified by the thermodynamic criteria. The influence of kinetically vs. thermodynamically bound waters on protein-protein interactions is also described.