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![[Figure 4]](ai5017fig4mag.jpg)
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Figure 4
hGSDMD-CTD–Peptide 2 binding interface and surface. (a) A close-up view of the hGSDMD interface at the exosite. The hydrogen bonds between GSDMD and Peptide 2 are shown as yellow dotted lines and hydrogen bonds to the other peptide molecule in the asymmetric unit are shown as gray dotted lines. Water molecules are shown as red crosses. (b) The surface of the hGSDMD exosite binding pocket colored by lipophilicity. The key residues of Peptide 2 that are involved in the interaction with hGSDMD are shown in stick representation. Green and purple colors indicate hydrophobic and hydrophilic surfaces, respectively. (c) The hydrophobic binding pocket is surrounded by acidic residues. hGSDMD is colored gray and the peptide key interaction residues are colored yellow and cyan, respectively. The blue cylinders with dashed lines represent hydrogen bonds. Longer cylinders indicate stronger hydrogen bonds. |
![[Figure 4]](ai5017fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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