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. 2022 Feb 3;12:1898. doi: 10.1038/s41598-022-05995-1

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© The Author(s) 2022

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Alingment and super position of the 3D structures of the E6-reference and its variants. (A) Multiple alignment of the sequence of E6 and its variants. Zinc finger domain 1 and 2 are highlighted in purple, PBM in blue and mutations are highlighted in pink. A super position of the secondary structure of all six proteins is shown in pink below the alignment. (B) 3D structure of E6-reference: violet, AAa variant: orange, AAc variant: red, E-G350, green, E-C188/G350: yellow, E-A176/G350: blue. The silver spheres indicate zinc molecules and the licorice residues correspond to C30, C33, C63, C66, C103, C106, C136 and C139, which make up two zinc finger domains in the proteins 3D structures. The orientation of the proteins is indicated by the axes, X: red, Y: green; Z: blue. (C) Visualization of amino acid changes: Q14H, D25N, I27R, H78Y and L83V are in licorice.