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. 2019 Oct 21;9:15076. doi: 10.1038/s41598-019-50701-3

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Variability in hNEDD4-WW3 binding site geometry. Uppers panels (a–d) show the surface depiction of the representative structures from the four most populated clusters in the apo-NEDD4-WW3 domain simulation. Lower panels show the surface representation of the hNEDD4-WW3 domain from the crystal structure of the ARRDC3 complex (4N7H)²⁸ (e), the lowest energy NMR models for the HTLV1 and Ebola complexes (this work 2KPZ and 2KQ0) (f,g) and the crystal structure of the apo NEDD4-WW3 domain (4N7F) (h). Residues in the xY pockets are colored in yellow, the xP pocket in light blue. Shown are the estimated sizes for the two pockets calculated with FPocket⁶⁸.