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. 2018 Aug 17;1:120. doi: 10.1038/s42003-018-0121-8

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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. 1 — Overall structure of human Dcytb. a Ribbon representation of the Dcytb homodimer. Each monomer consists of six α-helices (α1−α6). Both N- and C- termini are located on the cytoplasmic side. Each monomer contains two heme b molecules, coordinated by four highly conserved His residues in a six-coordinate low spin form. b The edge-to-edge distance between two heme molecules is 15.5 Å. c The environment of the heme bound to the cytoplasmic side of Dcytb is shown. d The environment of the heme bound to the apical side of Dcytb is shown