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![[Figure 3]](jb5065fig3mag.jpg)
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Figure 3
PR10-10 cap-loop conformations. The cap-loop conformations in PR10-10 crystal structures and their binding pockets. The cap loops and β2 strands are highlighted in blue. Calculated largest internal cavities (i.e. binding pockets) are shown in red and labeled with their volumes (Chwastyk et al., 2014  , 2016). Cysteine residues are shown in stick format and highlighted in yellow, whereas the corresponding Cys→Ser mutations are highlighted in red. The conserved PR10-10 homodimer is shown at the bottom with the displayed protomer in green and its partner in gray. The single protomers and the dimer have slightly different orientations in order to better showcase their features. The dimer interface along the β1 strand is indicated by a black line. |
![[Figure 3]](jb5065fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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