5VR3: BRS domain of BRAF

Crystal structure of the BRS domain of BRAF. Determined by X-ray diffraction at 2.1 Å resolution. Released 14 Feb 2018.

Method
X-ray diffraction
Resolution
2.1 Å
Organism
Homo sapiens
Chains
1
Atoms
510
Mol. weight
9.64 kDa
Released
14 Feb 2018

Explore 5VR3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 2 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix45-6521
α-helix76-9924

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
BrafAprotein88Homo sapiensP15056 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5VR3_1 BRAF (chains A)
GAMDPGGGGSSAADPAIPEEVWNIKQMIKLTQEHIEALLDKFGGEHNPPSIYLEAYEEYT
SKLDALQQREQQLLESLGNGTDFSVSSS

Primary citation

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:

Browse structure collections

About this viewer

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