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![[Figure 4]](ud5029fig4mag.jpg)
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Figure 4
CryoEM structure of SrBDH1. (a) Tetrameric assembly of SrBDH1. Density-modified cryoEM reconstructions at a contour level of 9.5 are shown for each of the four protomers in different shades of blue. Locations of very well defined water molecules are shown in red. (b) The same color-coding as in (a) but rotated by 90°. (c) Grouped B factor mapped onto the density. The color gradient is from blue to red corresponding to increasing B factors. In contrast to SoBDH2, the B-factor distribution is uniform. (d) The SrBDH1 structure in cartoon representation. The same view and color-coding are used as in (a). (e) Enlargement of the C-terminal end of αF with an alternate side-chain conformation of Ser179 and well defined water molecules, shown as red spheres. (f) C-terminal end of αH with Phe260 with a characteristic hole in the density for the aromatic ring system. (g) Double conformation of Arg74. The water molecule is at a distance of 2.5 Å from the guanidinium function of Arg74 in side-chain conformation Arg74(B). |
![[Figure 4]](ud5029fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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