Domain swapped E6AP C-lobe dimer. Determined by X-ray diffraction at 1.3 Å resolution. Released 26 Feb 2020.
Explore 6TGK in 3D Show helices and sheets RCSB PDB PDBe
6TGK contains 7 α-helices and 2 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 744-750 | 7 | |
| β-strand | 752-754 | 3 | 1 |
| α-helix | 762-772 | 11 | |
| α-helix | 776-787 | 12 | |
| α-helix | 792-793 | 2 | |
| α-helix | 797-799 | 3 | |
| β-strand | 803-805 | 3 | 1 |
| α-helix | 814-815 | 2 | |
| α-helix | 832-844 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin-protein ligase E3A | C | protein | 105 | Homo sapiens | Q05086 (AlphaFold model) |
>6TGK_1 Ubiquitin-protein ligase E3A (chains C) LDFQALEETTEYDGGYTRDSVLIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKLK MIIAKNGPDTERLPTSHTCFNVLLLPEYSSKEKLKERLLKAITYA
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 1 |
Water and common crystallization additives (ACT) are not listed.
Crystal structure of the catalytic C-lobe of the HECT-type ubiquitin ligase E6AP. Ries, L.K., Liess, A.K.L., Feiler, C.G. et al. Protein Sci (2020) 29:1550-1554. DOI 10.1002/pro.3832 · PubMed
Other PDB entries of the same protein (UniProt Q05086 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 6TGK directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.