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. 2022 Sep 20;37(1):1752–1764. doi: 10.1080/14756366.2022.2087645

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© 2022 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 6. — A shows diflapolin within the binding site of sEH. Red arrows signify hydrogen bond acceptor interactions, while green arrows mark hydrogen bond donor interactions. The yellow spheres represent hydrophobic contacts between protein and ligand. The urea moiety of diflapolin is bound to Asp335, Tyr383, Gln384, and in some poses Tyr466 (not shown). The two yellow rings mark the two hydrophobic cavities on both sides of the catalytic triad leading up to Leu408 and Trp473. B shows the most active molecule of the series 5b bound to sEH with hydrogen bonds to Tyr383, Tyr466, Asp335, and His524.