Crystal structure of the BRS domain of BRAF. Determined by X-ray diffraction at 2.1 Å resolution. Released 14 Feb 2018.
Explore 5VR3 in 3D Show helices and sheets RCSB PDB PDBe
5VR3 contains 2 α-helices and 0 β-strands across 1 chain. 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 | 45-65 | 21 | |
| α-helix | 76-99 | 24 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Braf | A | protein | 88 | Homo sapiens | P15056 (AlphaFold model) |
>5VR3_1 BRAF (chains A) GAMDPGGGGSSAADPAIPEEVWNIKQMIKLTQEHIEALLDKFGGEHNPPSIYLEAYEEYT SKLDALQQREQQLLESLGNGTDFSVSSS
MEK drives BRAF activation through allosteric control of KSR proteins. Lavoie, H., Sahmi, M., Maisonneuve, P. et al. Nature (2018) 554:549-553. DOI 10.1038/nature25478 · PubMed
Other PDB entries of the same protein (UniProt P15056 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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