Crystal structure of the second bromodomain H395R mutant of human BRD3. Determined by X-ray diffraction at 1.7 Å resolution. Released 20 Jan 2016.
Explore 5HFR in 3D Show helices and sheets RCSB PDB PDBe
5HFR contains 34 α-helices and 0 β-strands across 4 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 | 308-322 | 15 | |
| α-helix | 325-327 | 3 | |
| α-helix | 328-331 | 4 | |
| α-helix | 332-334 | 3 | |
| α-helix | 340-343 | 4 | |
| α-helix | 348-351 | 4 | |
| α-helix | 358-366 | 9 | |
| α-helix | 373-390 | 18 | |
| α-helix | 396-413 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 310-322 | 13 | |
| α-helix | 325-327 | 3 | |
| α-helix | 328-331 | 4 | |
| α-helix | 332-334 | 3 | |
| α-helix | 348-351 | 4 | |
| α-helix | 358-366 | 9 | |
| α-helix | 373-390 | 18 | |
| α-helix | 396-413 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 310-322 | 13 | |
| α-helix | 325-327 | 3 | |
| α-helix | 328-331 | 4 | |
| α-helix | 332-334 | 3 | |
| α-helix | 340-343 | 4 | |
| α-helix | 348-351 | 4 | |
| α-helix | 358-366 | 9 | |
| α-helix | 373-390 | 18 | |
| α-helix | 396-413 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Bromodomain-containing protein 3 | A, B, C, D | protein | 113 | Homo sapiens | Q15059 (AlphaFold model) |
>5HFR_1 Bromodomain-containing protein 3 (chains A, B, C, D) SMGKLSEHLRYCDSILREMLSKKHAAYAWPFYKPVDAEALELHDYHDIIKHPMDLSTVKR KMDGREYPDAQGFAADVRLMFSNCYKYNPPDREVVAMARKLQDVFEMRFAKMP
Crystal structure of the second bromodomain H395R mutant of human BRD3. Tallant, C., Lori, C., Pasquo, A. et al. To be published.
Other PDB entries of the same protein (UniProt Q15059 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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