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. 2019 Feb 8;294(15):6113–6129. doi: 10.1074/jbc.RA118.007014

Figure 4.

Figure 4.

Model of a NEDD4-type complex between the C-lobe of E6AP and ubiquitin, as required for thioester formation. Ubiquitin was modeled by structural superposition of the C-lobe of the ubiquitin-bound HECT domain of NEDD4 (PDB code 4BBN, chain A (18)) with the C-lobe of the HECT domain of E6AP (chain A, extracted from PDB code 1C4Z (30)), using the PyMOL Molecular Graphics System, Version 2.0, Schrödinger, LLC. Ubiquitin and the E6AP C-lobe are displayed in ribbon representation; the side chains of residues relevant for thioester formation are displayed as balls and sticks. The side chain of the catalytic cysteine, Cys-820, is also displayed. The backbone nitrogen atoms of additional residues that experience perturbations upon ubiquitin addition are shown as spheres.