Crystal structure of yeast E2 Ubiquitin-conjugating enzyme Ubc6 UBC domain. Determined by X-ray diffraction at 1.21 Å resolution. Released 20 Nov 2024.
Explore 9EWP in 3D Show helices and sheets RCSB PDB PDBe
9EWP contains 8 α-helices and 6 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 | 4-19 | 16 | |
| α-helix | 21-22 | 2 | |
| β-strand | 25-30 | 6 | 1 |
| β-strand | 33-42 | 10 | 1 |
| α-helix | 43-44 | 2 | |
| β-strand | 53-59 | 7 | 1 |
| α-helix | 68-69 | 2 | |
| β-strand | 70-73 | 4 | 1 |
| β-strand | 80 | 1 | 2 |
| α-helix | 104-116 | 13 | |
| β-strand | 124 | 1 | 2 |
| α-helix | 129-145 | 17 | |
| α-helix | 148-153 | 6 | |
| α-helix | 155-172 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin-conjugating enzyme E2 6 | A | protein | 178 | Saccharomyces cerevisiae | P33296 (AlphaFold model) |
>9EWP_1 Ubiquitin-conjugating enzyme E2 6 (chains A) MATKQAHKRLTKEYKLMVENPPPYILARPNEDNILEWHYIITGPADTPYKGGQYHGTLTF PSDYPYKPPAIRMITPNGRFKPNTRLCLSMSDYHPDTWNPGWSVSTILNGLLSFMTSDEA TTGSITTSDHQKKTLARNSISYNTFQNVRFKLIFPEVVQENVETLEKRKLDELPETGG
| ID | Name | Formula | Copies |
|---|---|---|---|
| CD | Cadmium ion | Cd | 4 |
Water and common crystallization additives (CL, NA, EDO) are not listed.
Determinants of chemoselectivity in ubiquitination by the J2 family of ubiquitin-conjugating enzymes. Swarnkar, A., Leidner, F., Rout, A.K. et al. EMBO J (2024) 43:6705-6739. DOI 10.1038/s44318-024-00301-3 · PubMed
Other PDB entries of the same protein (UniProt P33296 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 9EWP 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.