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. 2022 Dec 22;51(1):475–487. doi: 10.1093/nar/gkac1207

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© The Author(s) 2022. Published by Oxford University Press on behalf of Nucleic Acids Research.

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

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Figure 5. — NSP14 fragment screening results overview and details of MTase domain pockets. (A) Overview of all 72 fragments observed to bind to NSP14 from our fragment screen. The major pockets and potential sites of inhibition are labelled. (B) Surface view of fragments bound to the MTase active site, the right hand panel shows the ^7MeGpppG viewed from the same perspective for reference. (C) Surface view of pockets bound to a potential allosteric site of inhibition for the MTase activity. The black stick representation shows the contribution of a crystallographic symmetry mate to the upper left side of the pocket. The right hand panel shows the conformation of the equivalent loop (shown in Cyan) in the SARS-CoV NSP14/10 complex. This loop is involved in binding SAM, and the putative inhibitory potential of these fragments against MTase activity may stem from their prevention of this structural transition.