view article
Figure 2
Distinct features of the SaTatD structure. (a) Chains A and B are shown as ribbon diagrams within the transparent surface colored purple and cyan, respectively. The dimeric interface areas consisting of Loop′1–Loop2–Loop3 (i) and Loop1–Loop′2–Loop′3 (ii) are expanded in the right panel. The residues contributing to hydrogen-bonding interactions are labeled and shown as lines. The interactions are presented as dotted lines (red). (b) LigPlot diagram presenting hydrophilic (red dotted lines) and hydrophobic (pink spoked curves) interactions in the dimeric interface. (c) The cis-peptide bonds observed in the SaTatD structure. Each cis-peptide is enlarged in the right panel (i, ii and iii) and shown as a red trapezoid. The related residues are shown in ball-and-stick representation with 2mFo − DFc electron-density maps contoured at 2.0σ as a blue mesh.

IUCrJ
Volume 7| Part 3| May 2020| Pages 509-521
ISSN: 2052-2525
https://doi.org/10.1107/S2052252520003917