Overall structure of <i>B. distachyon</i> PDIL1-1 protein.

<p>The tertiary structure was predicted by the Phyre2 server, and the abb′xa′c (five domains and one linker) structure composition indicated similarity with the structure of human and yeast PDI. The -CXXC- catalytic sites are indicated by green and red spheres. The secondary structure is shown with α helixes in red, β sheets in yellow, and loops in green. Some important amino acid (glutamicacid–lysine charged pair and conserved arginine) are marked near each active site on the basis of the characteristics of human PDI.