Structure of Brdt bromodomain BD1 bound to a diacetylated histone H4 peptide. Determined by X-ray diffraction at 2.37 Å resolution. Released 22 Sept 2009.
Explore 2WP2 in 3D Show helices and sheets RCSB PDB PDBe
2WP2 contains 20 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 | 29-33 | 5 | |
| α-helix | 34-39 | 6 | |
| α-helix | 40-43 | 4 | |
| α-helix | 46-51 | 6 | |
| α-helix | 65-68 | 4 | |
| α-helix | 75-83 | 9 | |
| α-helix | 90-107 | 18 | |
| α-helix | 109 | 1 | |
| α-helix | 113-129 | 17 | |
| α-helix | 133-135 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 29-33 | 5 | |
| α-helix | 34-39 | 6 | |
| α-helix | 40-44 | 5 | |
| α-helix | 49-51 | 3 | |
| α-helix | 65-68 | 4 | |
| α-helix | 75-83 | 9 | |
| α-helix | 90-107 | 18 | |
| α-helix | 109 | 1 | |
| α-helix | 113-129 | 17 | |
| α-helix | 133-134 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Bromodomain testis-specific protein | A, B | protein | 120 | MUS MUSCULUS | Q91Y44 (AlphaFold model) |
| Histone H4 | P, Q | protein | 20 | MUS MUSCULUS | P62806 (AlphaFold model) |
>2WP2_1 BROMODOMAIN TESTIS-SPECIFIC PROTEIN (chains A, B) EYINTKKSGRLTNQLQFLQRVVLKALWKHGFSWPFQQPVDAVKLKLPDYYTIIKTPMDLN TIKKRLENKYYEKASECIEDFNTMFSNCYLYNKTGDDIVVMAQALEKLFMQKLSQMPQEE
>2WP2_2 HISTONE H4 (chains P, Q) SGRGKGGKGLGKGGAKRHRK
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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