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. 2013 Apr 11;69(Pt 5):830–837. doi: 10.1107/S0907444913002023

Figure 2.

Figure 2

Structural comparison of the active sites of Deg5 (S266A), Deg1 and HtrA1. (a) Catalytic triad of Deg5 (S266A) (yellow). Hydrogen bonds between His147 and Asp188 and between His147 and Thr284 are presented as black dashed lines. The catalytic triad and Thr284 from loop L2 are shown in stick mode. (b) Alternative conformation of His147. His147 is displayed together with electron density calculated using 2F o − F c coefficients and contoured at 0.7σ as a blue mesh. (c) Structural comparison of catalytic triads and activation loops of Deg5 (S266A), Deg1 (PDB entry 3qo6) and HtrA1 (PDB entry 3num; Truebestein et al., 2011 ▶). Catalytic triads are shown in stick mode and are coloured yellow. Loops LD, L1, L2 and L3 are coloured red, blue, green and magenta, respectively.