Rad18 ubiquitin ligase RING domain structure. Determined by X-ray diffraction at 1.8 Å resolution. Released 11 May 2011.
Explore 2Y43 in 3D Show helices and sheets RCSB PDB PDBe
2Y43 contains 9 α-helices and 14 β-strands across 2 chains. 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 | 11-16 | 6 | |
| α-helix | 17-22 | 6 | |
| β-strand | 24 | 1 | 1 |
| β-strand | 31 | 1 | 1 |
| β-strand | 35-37 | 3 | 2 |
| β-strand | 44-46 | 3 | 2 |
| α-helix | 47-54 | 8 | |
| β-strand | 59 | 1 | 3 |
| β-strand | 66 | 1 | 3 |
| α-helix | 69-71 | 3 | |
| β-strand | 73-74 | 2 | 2 |
| α-helix | 76-90 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 16-22 | 7 | |
| β-strand | 24 | 1 | 4 |
| β-strand | 31 | 1 | 4 |
| β-strand | 35-37 | 3 | 5 |
| β-strand | 44-46 | 3 | 5 |
| α-helix | 47-54 | 8 | |
| β-strand | 59 | 1 | 6 |
| β-strand | 66 | 1 | 6 |
| α-helix | 69-71 | 3 | |
| β-strand | 73-74 | 2 | 5 |
| α-helix | 76-93 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| E3 ubiquitin-protein ligase RAD18 | A, B | protein | 99 | HOMO SAPIENS | Q9NS91 (AlphaFold model) |
>2Y43_1 E3 UBIQUITIN-PROTEIN LIGASE RAD18 (chains A, B) MDSLAESRWPPGLAVMKTIDDLLRCGICFEYFNIAMIIPQCSHNYCSLCIRKFLSYKTQC PTCCVTVTEPDLKNNRILDELVKSLNFARNHLLQFALES
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 4 |
Symmetry and Asymmetry of the Ring-Ring Dimer of Rad18. Huang, A., Hibbert, R.G., De Jong, R.N. et al. J Mol Biol (2011) 410:424. DOI 10.1016/J.JMB.2011.04.051 · PubMed
Other PDB entries of the same protein (UniProt Q9NS91 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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