Abstract
It is tempting to use standard protonation states for the analysis of protein–ligand interactions. Two different pKa calculation methods, PROPKA (protein pKa) and MCCE (multi conformation continuum electrostatics), were applied to challenge this convenient behavior. As data basis, we selected five recently approved drugs for which structural information of the protein–drug complex is available. We analyzed the pKa calculations in terms of a measure termed BIPS (binary protonation states) recently introduced by us. Both methods agree in detecting the majority of the sites with atypical BIPS values. However, when using only one method, some of the atypcial BIPS value would have been missed. Therefore, we recommend using both methods to set such an interpretation on a solid basis.
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