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Figure 3
Views of the asparagine residues with glycosylations (in mouse EPDR1) (a, b) and the Ca2+-binding site (in frog EPDR1) (c) with experimental electron densities. (a) In mouse EPDR1, Asn130 is clearly seen to have a NAG modification. A stimulated-annealing OMIT map of Fo − Fc difference density was contoured at 1.1σ. (b) Also in mouse EPDR1, Asn182 is clearly seen to have a NAG–FUC–NAG modification. A stimulated-annealing OMIT map of Fo − Fc difference density was contoured at 1.1σ. (c) In frog EPDR1, Ca2+ was found to be octahedrally coordinated by four water molecules and other nearby atoms of Asp121 and Pro122. The water molecules coordinated to Ca2+ are further stabilized by tight hydrogen-bonding interactions with the nearby residues Asp124, Glu175 and Tyr177. A stimulated-annealing OMIT map of Fo − Fc difference density was contoured at 3.0σ.

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