Crystal structure of phosphorylated ETS-1 DNA binding and autoinhibitory domains (276-441). Determined by X-ray diffraction at 2.6 Å resolution. Released 20 Aug 2014.
Explore 3WU0 in 3D Show helices and sheets RCSB PDB PDBe
3WU0 contains 20 α-helices and 8 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 | 304-309 | 6 | |
| α-helix | 317-319 | 3 | |
| α-helix | 323-330 | 8 | |
| α-helix | 335-336 | 2 | |
| α-helix | 337-345 | 9 | |
| α-helix | 348-350 | 3 | |
| β-strand | 354-356 | 3 | 1 |
| β-strand | 362-365 | 4 | 1 |
| α-helix | 368-378 | 11 | |
| α-helix | 386-398 | 13 | |
| β-strand | 402-404 | 3 | 1 |
| α-helix | 405 | 1 | |
| β-strand | 411-414 | 4 | 1 |
| α-helix | 418-422 | 5 | |
| α-helix | 426-432 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 304-313 | 10 | |
| α-helix | 323-330 | 8 | |
| α-helix | 335-336 | 2 | |
| α-helix | 337-345 | 9 | |
| α-helix | 348-350 | 3 | |
| β-strand | 355-356 | 2 | 2 |
| β-strand | 362-364 | 3 | 2 |
| α-helix | 368-378 | 11 | |
| α-helix | 387-398 | 12 | |
| β-strand | 402-404 | 3 | 2 |
| β-strand | 411-414 | 4 | 2 |
| α-helix | 418-422 | 5 | |
| α-helix | 426-432 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein C-ets-1 | A, B | protein | 166 | Homo sapiens | P14921 (AlphaFold model) |
>3WU0_1 Protein C-ets-1 (chains A, B) SLQRVPSYDSFDSEDYPAALPNHKPKGTFKDYVRDRADLNKDKPVIPAAALAGYTGSGPI QLWQFLLELLTDKSCQSFISWTGDGWEFKLSDPDEVARRWGKRKNKPKMNYEKLSRGLRY YYDKNIIHKTAGKRYVYRFVCDLQSLLGYTPEELHAMLDVKPDADE
A novel allosteric mechanism on protein-DNA interactions underlying the phosphorylation-dependent regulation of Ets1 target gene expressions. Shiina, M., Hamada, K., Inoue-Bungo, T. et al. J Mol Biol (2015) 427:1655-1669. DOI 10.1016/j.jmb.2014.07.020 · PubMed
Other PDB entries of the same protein (UniProt P14921 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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