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. 2023 Jan 9;9:1058569. doi: 10.3389/fcvm.2022.1058569

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Copyright © 2023 Yang, Wang, Zhang, Fan, Zheng, Xiao, Chen, Xiao and Liu.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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The structure analysis of SerRS variants using PyMOL 2.5.2, and the structure is optimized by molecule dynamics simulation to acquire the most stable configurations. The hydrogen bonds are marked with yellow dashes. (A) Configuration of SerRS wild type. (B) Configuration of SerRS p.Arg227Gln variant. (C) Configuration of SerRS p.Arg402His variant. (D) Configuration of SerRS p.Arg402His/p.Arg227Gln variants. All variants did not cause significant structure damage to SerRS. However, p.Arg227Gln and p.Arg402His/p.Arg227Gln variants lost the hydrogen bond of Arg-227 with Thr-335 and Glu-332, while acquired the hydrogen bond with His-346. p.Arg402His and p.Arg402His/p.Arg227Gln lost the hydrogen bond and ionic bonds between Arg-402 and Asp-390.