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![[Figure 2]](no5182fig2mag.jpg)
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Figure 2
(a) Overall topology of Δ18PA1624 with α-helical elements colored yellow and β-strands red. The two domains are connected via a long linker stretching from β9 to α3. The light blue connection indicates a disulfide bridge. (b) The amino-acid conservation was calculated with ConSurf (Ashkenazy et al., 2016  ) and plotted on the protein structure. (c) Ribbon representation of Δ18PA1624. The same coloring scheme as in (a) was used. The circle indicates the location of the hydrophobic cavity shown from different angles in (d). (d) The hydrophobic cavity location and its shape are depicted in three different orientations. |
![[Figure 2]](no5182fig2.jpg)
 | STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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