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. 2020 Jun 12;103(2):368–377. doi: 10.1093/biolre/ioaa097

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© The Author(s) 2020. Published by Oxford University Press on behalf of Society for the Study of Reproduction.

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 reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Modeling of potential allosteric site. (A) Full-length WEE2 homology model. FTMap was used on a Phyre2 homology model to identify a region (red) where multiple solvent species (yellow) found energy minima, indicating a potential binding pocket. Orthosteric ATP site is approximated by alignment and extraction of ATPgammaS (non-hydrolyzable ATP analog, purple) from enzyme structure in the same family (EC 2.7.10.2; PDB ID: 5c03). (B) WEE2 kinase domain crystal structure. FTMap was again used to locate potential binding sites in the crystal structure (PDB ID: 5vdk) outside of the orthosteric site, represented by the same ATPgammaS molecule extracted from PDB ID: 5c03 for consistency in orientation. This analysis revealed a similar site (red), which was also identified by FTSite and SiteMap, that engaged with several non-ATP associated side chains.