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. 2018 Dec 4;12:128. doi: 10.1186/s13065-018-0497-z

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© The Author(s) 2018

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 57 — Most stable binding of C53₅₃ with respect to hMAO-A (left side) and hMAO-B (right side). Ligands are shown in CPK colored sticks, interacting residues are coloured in green (hMAO-A) or orange (hMAO-B) carbons in sticks rendering. FAD is reported in spacefill with green (hMAO-A) or orange (hMAO-B) carbon atoms. Non-interacting aminoacids are in transparent green (hMAO-A) or orange (hMAO-B) cartoon notation. Inhibitor-enzyme hydrogen bonds are reported in cyan dashed lines [89]