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Figure 13
Nuclear density for the active site of the endothiapepsin–inhibitor complex. Asp32 is deprotonated, likely forming a low-barrier hydrogen bond with the gem-diol inhibitor, while Asp215 is protonated, acting as a hydrogen-bond donor to the inhibitor. Reprinted with permission from Coates et al. (2008BB15), J. Am. Chem. Soc. 130, 7235–7237. Copyright (2008) American Chemical Society.

IUCrJ
Volume 4| Part 1| January 2017| Pages 72-86
ISSN: 2052-2525
https://doi.org/10.1107/S205225251601664X