Unusual Molecular Interactions from the PDB
Protein-ligand interactions are driven predominantly by strong hydrogen-bonding interactions, de-solvation energetics, and other entropic considerations including ligand lipophilicity. However, the combination of many weaker interactions can contribute to potency, and are often necessary to obtain selectivity when targets and anti-targets have very similar binding pockets. Weak interactions such as Dunitz interactions, polarized C-H hydrogen bonding…
