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. 2019 Oct 30;10:4939. doi: 10.1038/s41467-019-12718-0

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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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Fig. 3 — Structure of OLPVRII protomer, retinal-binding pocket and extracellular part. a Overall side view of protomer A. Helices F and G are hidden for clarity. Hydrophobic−hydrophilic boundaries of the membrane are shown with gray lines. b Detailed view of the extracellular part. c Detailed view of the retinal-binding pocket. Residues comprising the walls of the pocket are colored teal. d Detailed view of the RSB region. Helices A and B are hidden for clarity. Cavities inside the protein protomer are colored pink. Lys195 and covalently bound retinal are colored cyan