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. 2015 Jan 7;83(2):351–372. doi: 10.1002/prot.24730

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© 2014 The Authors. Proteins: Structure, Function, and Bioinformatics Published by Wiley Periodicals, Inc.

This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made.

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Fraction of electrostatic contributions to relative binding affinity losses for randomly chosen, mono‐specific compounds that were extra small (A), extra large (B), and extra polar (C). Each block represents a pair of protein (on the x‐axis) and inhibitor (on the y‐axis). Warmer color represents more contribution from electrostatics. The deepest red color indicates that hydrogen‐bond groups on corresponding inhibitors could not be all satisfied. The black color indicates that corresponding compounds do not fit in the binding site geometrically. The white color indicates that the compound binds the corresponding target.