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. Author manuscript; available in PMC: 2020 Jul 15.
Published in final edited form as: Nature. 2020 Jan 15;577(7791):572–575. doi: 10.1038/s41586-019-1909-5

Extended Data Figure 5. Structure of SIRV1 gp29 bound to cA4.

Extended Data Figure 5

a and b, Orthogonal views of SIRV1 gp29 dimer in complex with cA4. The protein monomers are coloured blue and orange, with catalytic residue H47 from the apo structure shown in salmon. cA4 is shown in spacefill with green, blue, red and orange representing carbon, nitrogen, oxygen and phosphorus atoms, respectively. Conserved residues (Extended data figure 1) in the AcrIII-1 family are indicated and discussed in the text. (c) Interactions between each monomer of the SIRV1 dimer (orange and blue), with cA4 shown in green. (d) Schematic showing the interaction. Dotted lines represent hydrogen bonds, with the distance annotated. Spheres represent water molecules.