Ets1 cooperative binding to widely separated sites on promoter DNA. Determined by X-ray diffraction at 3.0 Å resolution. Released 4 Apr 2012.
Explore 3RI4 in 3D Show helices and sheets RCSB PDB PDBe
3RI4 contains 16 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 | 304-312 | 9 | |
| α-helix | 323-330 | 8 | |
| α-helix | 337-346 | 10 | |
| α-helix | 348-350 | 3 | |
| β-strand | 355-356 | 2 | 1 |
| β-strand | 362-364 | 3 | 1 |
| α-helix | 368-378 | 11 | |
| α-helix | 386-398 | 13 | |
| β-strand | 402-404 | 3 | 1 |
| β-strand | 411-414 | 4 | 1 |
| α-helix | 418-422 | 5 | |
| α-helix | 426-432 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 304-312 | 9 | |
| α-helix | 323-330 | 8 | |
| α-helix | 337-344 | 8 | |
| α-helix | 348-350 | 3 | |
| β-strand | 355-356 | 2 | 2 |
| β-strand | 362-364 | 3 | 2 |
| α-helix | 368-378 | 11 | |
| α-helix | 386-398 | 13 | |
| 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 |
|---|---|---|---|---|---|
| Isoform Ets-1 p27 of Protein C-ets-1 | A, D | protein | 163 | Homo sapiens | P14921 (AlphaFold model) |
| TCR alpha promoter DNA | B, E | DNA | 16 | ||
| TCR alpha promoter DNA | C, F | DNA | 16 |
>3RI4_1 Isoform Ets-1 p27 of Protein C-ets-1 (chains A, D) MVPSYDSFDYEDYPAALPNHKPKGTFKDYVRDRADLNKDKPVIPAAALAGYTGSGPIQLW QFLLELLTDKSCQSFISWTGDGWEFKLSDPDEVARRWGKRKNKPKMNYEKLSRGLRYYYD KNIIHKTAGKRYVYRFVCDLQSLLGYTPEELHAMLDVKPDADE
>3RI4_2 TCR alpha promoter DNA (chains B, E) GGAAGCCACATCCTCT
>3RI4_3 TCR alpha promoter DNA (chains C, F) CAGAGGATGTGGCTTC
Structural basis of ets1 cooperative binding to widely separated sites on promoter DNA. Babayeva, N.D., Baranovskaya, O.I., Tahirov, T.H. PLoS One (2012) 7:e33698-e33698. DOI 10.1371/journal.pone.0033698 · 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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