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. Author manuscript; available in PMC: 2018 Jan 6.
Published in final edited form as: Nature. 2017 Jul 6;548(7667):352–355. doi: 10.1038/nature23314

Extended Data Figure 8. Potential Hrd3 binding surfaces for substrate and partners.

Extended Data Figure 8

a, Groove at the inner surface of Hrd3 (encircled), located at the junction of the N-terminal (residues 187-199), middle (residues 507-521), and C-terminal (residues 539-560, 593-595) domains. The left panel shows a space-filling model with conserved amino acids shown in orange to red (scores 7-9 in the program Consurf). Hrd1 is shown in ribbon presentation. The right panel shows the same view with Hrd3 in cartoon presentation. Helices containing the conserved residues are shown as ribbons. Some residues are labeled for orientation. b, The left panel shows three conserved surface grooves on the outer surface of Hrd3 (encircled), with conserved residues colored as in a. The right panel shows the same view with helices containing conserved residues in ribbon presentation.