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![[Figure 5]](jv5010fig5mag.jpg)
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Figure 5
Structure of mutant RDM1-18 determined at 1.20 Å resolution. 2Fo − Fc electron-density map (contour level 1.50σ) near (a) the catalytic Thr179 and (b) the sodium-binding loop in chain B; the sodium cation is colored violet. (c) 2Fo − Fc electron-density map (contour level 1.50σ) around the mutation sites in chain B. (d) Conformation of Trp211 in chain B; the presence of the bulky aromatic side chain does not affect the pattern of hydrogen bonds near the Thr triad. (e) Alternative conformations of Trp211 and the neighboring fragment Thr232–Glu234 in chain D. In all panels, the mutation sites are marked in frames. Water molecules are shown as red spheres and hydrogen bonds as dashed lines. |
![[Figure 5]](jv5010fig5.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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