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. 2018 Oct 18;9:4337. doi: 10.1038/s41467-018-06817-7

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© The Author(s) 2018

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. 4 — Substrate-binding site above the porphyrin. a Sideview of the extracellular side of the TMD of a STEAP4 protomer (shown in grey). The difference density is contoured at 18σ. b Positively charged amino acid ring that surrounds the substrate density, as viewed from the extracellular side of the membrane. Residue R318 belongs to an adjacent STEAP4 protomer. The difference density is contoured at 18σ. The shown residues display variable conservation as basic amino acids (percentage in brackets) throughout 607 STEAP orthologs:¹⁵ R221 (96%), R237 (87%), R245 (72%), R314 (98%), R318 (97%) R320 (48%), K404 (48%), R405 (94%), R413 (72%)