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. 2018 Oct 9;15(10):1255–1267. doi: 10.1080/15476286.2018.1526541

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© 2018 The Author(s). Published by Taylor & Francis.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.

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Figure 4. — The structure of the hNOCT EEP catalytic domain (aa 120–431) reveals a conserved hydrolase fold. A) Overview of the 1.48 Å resolution structure (6BT1) [71]. Active site residues are shown; one Mg²⁺ ion (gray) is coordinated to E195 and ordered water molecules (not pictured). B) Magnified view of active site from (A). C) Overview of 2.48 Å resolution structure (6BT2) [71] with active site (salmon) and basic patch (cyan) residues shown. Two Mg²⁺ ions (gray), coordinated to E195 and D324, and one SO₄ ^2–ion (yellow) bound to lysine side chains adjacent to the active site are shown. D) Magnified view of active site and adjacent basic patch shown in (C).