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. 2016 Nov 15;173(1):417–433. doi: 10.1104/pp.16.01426

Figure 3.

Figure 3.

Structural alignment of PviPRX9 with seven CIIIPRXs from the Research Collaboratory for Structural Bioinformatics PDB. Secondary structural elements were labeled with helices indicated by spirals and β-sheets indicated by arrows. The secondary structure was letter mapped according to the system laid out by Schuller et al. (1996). Residues coordinating with the two conserved Ca2+ atoms are indicated with plus signs. The conserved P-X-P-X motif is outlined with a box. The Cys residues participating in conserved disulfides are numbered according to the corresponding Cys. Amino acids with 75% or greater identity in the alignment are highlighted in gray, and the conserved Cys residues are highlighted in black.