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. 2015 Nov 3;5:16056. doi: 10.1038/srep16056

Figure 5. Structural comparison between UbcA1 and human Ube2w.

Figure 5

(A) Structure superimposition of the UbcA1 structure (red) and the crystal structure of Ube2w with the PDB code of 2A7L (blue) showing inconsistent N-terminal regions (residues 1–32) due to deviation of the latter structure from the canonical Ubc fold. (B) The dimeric model of UbcA1 displaying the protein-protein interface at the C-terminal segment and helix α3 in particular. (C) The dimeric model of 2A7L showing the interface formed by two loops, L3 and L6. (D) Structure superimposition of UbcA1 (red) and a recent NMR model of Ube2w with PDB code 2MT6 (blue). Both adopt the canonical fold except for a C-terminal peptide covering the last helix (α3). For clarity, only two models from the NMR ensemble are shown.