Crystal structure of the BRS domain of BRAF in complex with the CC-SAM domain of KSR1. Determined by X-ray diffraction at 1.75 Å resolution. Released 14 Feb 2018.
Explore 5VYK in 3D Show helices and sheets RCSB PDB PDBe
5VYK contains 24 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 | 34-61 | 28 | |
| α-helix | 67-93 | 27 | |
| α-helix | 101-104 | 4 | |
| α-helix | 106 | 1 | |
| α-helix | 108 | 1 | |
| α-helix | 109-115 | 7 | |
| α-helix | 120-124 | 5 | |
| α-helix | 132-137 | 6 | |
| α-helix | 140-149 | 10 | |
| α-helix | 154-170 | 17 | |
| α-helix | 1043-1068 | 26 | |
| α-helix | 1076-1103 | 28 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 34-61 | 28 | |
| α-helix | 67-93 | 27 | |
| α-helix | 101-104 | 4 | |
| α-helix | 106 | 1 | |
| α-helix | 108 | 1 | |
| α-helix | 109-115 | 7 | |
| α-helix | 120-124 | 5 | |
| α-helix | 132-137 | 6 | |
| α-helix | 140-149 | 10 | |
| α-helix | 154-170 | 17 | |
| α-helix | 1043-1068 | 26 | |
| α-helix | 1076-1104 | 29 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Chimera protein of BRS domain of BRAF and CC-SAM domain of KSR1,Serine/threonine-protein kinase… | A, C | protein | 232 | Homo sapiens | P15056 (AlphaFold model), Q8IVT5 (AlphaFold model) |
>5VYK_1 Chimera protein of BRS domain of BRAF and CC-SAM domain of KSR1,Serine/threonine-protein kinase B-raf (chains A, C) GAMEGGAGAAASRALQQCGQLQKLIDISIGSLRGLRTKCAVSNDLTQQEIRTLEAKLVRY ICKQRQCKLSVAPGERTPELNSYPRFSDWLYTFNVRPEVVQEIPRDLTLDALLEMNEAKV KETLRRCGASGDECGRLQYALTCLRKVTGGSGSGSGSSSAADPAIPEEVWNIKQMIKLTQ EHIEALLDKFGGEHNPPSIYLEAYEEYTSKLDALQQREQQLLESLGNGTDFS
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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