Molecular structure of the core of amyloid-like fibrils formed by residues 111-214 of FUS. Determined by electron microscopy at 2.62 Å resolution. Released 7 Oct 2020.
Explore 6XFM in 3D Show helices and sheets RCSB PDB PDBe
6XFM contains 0 α-helices and 32 β-strands across 8 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 | 3-13 | 11 | 1 |
| β-strand | 22 | 1 | 2 |
| β-strand | 25-26 | 2 | 3 |
| β-strand | 29-39 | 11 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| RNA-binding protein FUS | 1, 2, 3, 4, 5, 6, 7, 8 | protein | 104 | Homo sapiens | P35637 (AlphaFold model) |
>6XFM_1 RNA-binding protein FUS (chains 1, 2, 3, 4, 5, 6, 7, 8) GSYGSSSQSSSYGQPQSGSYSQQPSYGGQQQSYGQQQSYNPPQGYGQQNQYNSSSGGGGG GGGGGNYGQDQSSMSSGGGSGGGYGNQDQSGGGGSGGYGQGDRG
Molecular structure and interactions within amyloid-like fibrils formed by a low-complexity protein sequence from FUS. Lee, M., Ghosh, U., Thurber, K.R. et al. Nat Commun (2020) 11:5735-5735. DOI 10.1038/s41467-020-19512-3 · 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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