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Figure 1
The overall structures of human, mouse and frog EPDR1. A ribbon diagram of human EPDR1 is shown (in yellow) with secondary-structure elements indicated. The locations of cysteines (C1–C6) and the disulfide bonds are also shown. A ribbon diagram of mouse EPDR1 is shown (in green) with two asparagine residues and their NAG glycosylation shown as stick models. Although other types of glycosylation were observed at Asn182, only NAG is shown for clarity (see Fig. 3[link] for more on glycosylation). A ribbon diagram of frog EPDR1 is shown (in blue) with Ca2+ ions (shown as spheres), four Ca2+-binding waters (shown as spheres) and direct Ca2+-interacting residues (shown in stick representation). The details of the interaction network stabilizing the bound Ca2+ ions in frog EPDR1 are shown in Fig. 3[link](c). Note that the same colors will be used throughout the figures. The superposed structures of the three EPDR1s are also shown. The superimposed EPDR1 structures show Cα r.m.s.d.s of 0.8 Å (human versus mouse), 1.1 Å (human versus frog) and 1.1 Å (mouse versus frog).

IUCrJ
Volume 6| Part 4| July 2019| Pages 729-739
ISSN: 2052-2525
https://doi.org/10.1107/S2052252519007668