Molecular structure of FUS low sequence complexity domain protein fibrils. Determined by solid-state NMR. Released 27 Sept 2017.
Explore 5W3N in 3D Show helices and sheets RCSB PDB PDBe
5W3N contains 0 α-helices and 81 β-strands across 9 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 |
|---|---|---|---|
| β-strand | 38-40 | 3 | 1 |
| β-strand | 44-45 | 2 | 2 |
| β-strand | 52 | 1 | 3 |
| β-strand | 61-64 | 4 | 4 |
| β-strand | 67-70 | 4 | 5 |
| β-strand | 78 | 1 | 6 |
| β-strand | 84 | 1 | 7 |
| β-strand | 87 | 1 | 8 |
| β-strand | 93-95 | 3 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| RNA-binding protein FUS | A, B, C, D, E, F, G, H, I | protein | 241 | Homo sapiens | P35637 (AlphaFold model) |
>5W3N_1 RNA-binding protein FUS (chains A, B, C, D, E, F, G, H, I) MSYYHHHHHHDYDIPTTENLYFQGAMDPASNDYTQQATQSYGAYPTQPGQGYSQQSSQPY GQQSYSGYSQSTDTSGYGQSSYSSYGQSQNTGYGTQSTPQGYGSTGGYGSSQSSQSSYGQ QSSYPGYGQQPAPSSTSGSYGSSSQSSSYGQPQSGSYSQQPSYGGQQQSYGQQQSYNPPQ GYGQQNQYNSSSGGGGGGGGGGNYGQDQSSMSSGGGSGGGYGNQDQSGGGGSGGYGQQDR G
Structure of FUS Protein Fibrils and Its Relevance to Self-Assembly and Phase Separation of Low-Complexity Domains. Murray, D.T., Kato, M., Lin, Y. et al. Cell (2017) 171:615-627.e16. DOI 10.1016/j.cell.2017.08.048 · PubMed
Other PDB entries of the same protein (UniProt P35637 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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