The total interaction for a ligand bound to a protein can be broken down at the atomic level, then further in types of atomic interactions. Distributions of any can be calculated from large sets of docking runs. There are many reasons why this information is relevant. A chemical interpretation of the individual atomic binding characterizes overall protein-ligand binding. Identifying badly fitting atoms can be used in improved molecular design. Identifying atom and regions of good interaction can explain binding in terms of positional attachment and longevity of the ligand semi-bound state (in an on-/offdynamic setting).