Structure of Brdt bromodomain 2 bound to an acetylated histone H3 peptide. Determined by X-ray diffraction at 2.1 Å resolution. Released 22 Sept 2009.
Explore 2WP1 in 3D Show helices and sheets RCSB PDB PDBe
2WP1 contains 18 α-helices and 0 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 | 264-282 | 19 | |
| α-helix | 285-287 | 3 | |
| α-helix | 288-291 | 4 | |
| α-helix | 292-294 | 3 | |
| α-helix | 300-303 | 4 | |
| α-helix | 308-311 | 4 | |
| α-helix | 318-326 | 9 | |
| α-helix | 333-350 | 18 | |
| α-helix | 356-372 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 266-282 | 17 | |
| α-helix | 285-287 | 3 | |
| α-helix | 288-291 | 4 | |
| α-helix | 292-294 | 3 | |
| α-helix | 300-303 | 4 | |
| α-helix | 308-311 | 4 | |
| α-helix | 318-326 | 9 | |
| α-helix | 333-350 | 18 | |
| α-helix | 356-373 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Bromodomain testis-specific protein | A, B | protein | 126 | MUS MUSCULUS | Q91Y44 (AlphaFold model) |
| Histone H3 | P, Q | protein | 10 | MUS MUSCULUS | P68433 (AlphaFold model) |
>2WP1_1 BROMODOMAIN TESTIS-SPECIFIC PROTEIN (chains A, B) QQQHKVLKTVKVTEQLKHCSEILKEMLAKKHLPYAWPFYNPVDADALGLHNYYDVVKNPM DLGTIKGKMDNQEYKDAYEFAADVRLMFMNCYKYNPPDHEVVAMARTLQDVFELHFAKIP DEPIES
>2WP1_2 HISTONE H3 (chains P, Q) KAPRKQLATK
Cooperative Binding of Two Acetylation Marks on a Histone Tail by a Single Bromodomain. Moriniere, J., Rousseaux, S., Steuerwald, U. et al. Nature (2009) 461:664. DOI 10.1038/NATURE08397 · PubMed
Other PDB entries of the same protein (UniProt Q91Y44 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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