Crystal structure analysis of the N-terminal bromodomain of human BRD2 complexed with acetylated histone H4 peptide. Determined by X-ray diffraction at 2.3 Å resolution. Released 7 Aug 2007.
Explore 2DVR in 3D Show helices and sheets RCSB PDB PDBe
2DVR contains 26 α-helices and 4 β-strands across 5 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 | 11-15 | 5 | |
| α-helix | 16-21 | 6 | |
| α-helix | 22-25 | 4 | |
| α-helix | 31-33 | 3 | |
| α-helix | 39-42 | 4 | |
| α-helix | 47-50 | 4 | |
| α-helix | 57-65 | 9 | |
| α-helix | 72-89 | 18 | |
| β-strand | 94 | 1 | 1 |
| α-helix | 95-112 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-15 | 5 | |
| α-helix | 16-21 | 6 | |
| α-helix | 22-25 | 4 | |
| α-helix | 31-33 | 3 | |
| α-helix | 39-42 | 4 | |
| α-helix | 47-50 | 4 | |
| α-helix | 57-65 | 9 | |
| α-helix | 72-89 | 18 | |
| β-strand | 94 | 1 | 2 |
| α-helix | 95-111 | 17 | |
| α-helix | 114-117 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-15 | 5 | |
| α-helix | 16-21 | 6 | |
| α-helix | 22-26 | 5 | |
| α-helix | 47-50 | 4 | |
| α-helix | 57-65 | 9 | |
| α-helix | 72-89 | 18 | |
| α-helix | 95-111 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 14 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| bromodomain-containing protein 2 | A, B, C | protein | 122 | Homo sapiens | P25440 (AlphaFold model) |
| histone H4 | P, Q | protein | 15 | P02309 (AlphaFold model) |
>2DVR_1 bromodomain-containing protein 2 (chains A, B, C) GRVTNQLQYLHKVVMKALWKHQFAWPFRQPVDAVKLGLPDYHKIIKQPMDMGTIKRRLEN NYYWAASECMQDFNTMFTNCYIYNKPTDDIVLMAQTLEKIFLQKVASMPQEEQELVVTIP KN
>2DVR_2 histone H4 (chains P, Q) SGRGKGGKGLGKGGA
Structural Basis for Acetylated Histone H4 Recognition by the Human BRD2 Bromodomain. Umehara, T., Nakamura, Y., Jang, M.K. et al. J Biol Chem (2010) 285:7610-7618. DOI 10.1074/jbc.M109.062422 · PubMed
Other PDB entries of the same protein (UniProt P25440 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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