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. 2015 Mar 28;10:38. doi: 10.1186/s13023-015-0248-3

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© Sirrs et al.; licensee BioMed Central. 2015

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 credited. 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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Modeled structural environments of the disease-causing mutations in FAAH2. Modeled structure of human FAAH2. The protein backbone is shown as a cartoon (white) with the side chains of A458 (green) and the catalytic triad residues (K131, S206, S230; orange) shown as sticks. (B) Additional interactions formed by the p.Ala458Ser mutation. Potential hydrogen bonds are observed between the side chain of Ser458 (green sticks) and the side chain of N195 or the carbonyl oxygens of I202 and F237 (cyan sticks). Distances in angstroms between interacting atoms are shown in dark red.