Protein-protein interactions are key to understand biological processes at the molecular level. As a complement to experimental characterization of protein interactions, computational docking methods have become useful tools for the structural and energetics modeling of protein-protein complexes. A key aspect of such algorithms is the use of scoring functions to evaluate the generated docking poses and try to identify the best models. When the scoring functions are based on energetic considerations, they can help not only to provide a reliable structural model for the complex, but also to describe energetic aspects of the interaction. This is the case of the scoring function used in pyDock, a combination of electrostatics, desolvation and van der Waals energy terms. Its correlation with experimental binding affinity values of protein-protein complexes was explored in the past, but the per-residue decomposition of the docking energy was never systematically analyzed.Here we present pyDockEneRes, a web server that provides pyDock docking energy partitioned at the residue level, giving a much more detailed description of the docking energy landscape. Additionally, pyDockEneRes computes the contribution to the docking energy of the side-chain atoms. This fast approach can be applied to characterize a complex structure in order to identify energetically relevant residues (hot-spots) and estimate binding affinity changes upon mutation to alanine.The server does not require registration by the user and is freely accessible for academics at https://life.bsc.es/pid/pydockeneres.Supplementary data are available at Bioinformatics online.