6XFM: RNA-binding protein FUS

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.

Method
Electron microscopy
Resolution
2.62 Å
Organism
Homo sapiens
Chains
8
Atoms
2,360
Mol. weight
80.2 kDa
Released
7 Oct 2020

Explore 6XFM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chains 1, 2, 3, 4, 5, 6, 7 and 8: 0 helices, 4 β-strands

ElementResiduesLengthSheet
β-strand3-13111
β-strand2212
β-strand25-2623
β-strand29-39114

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
RNA-binding protein FUS1, 2, 3, 4, 5, 6, 7, 8protein104Homo sapiensP35637 (AlphaFold model)
Sequence of entity 1 (1, 2, 3, 4, 5, 6, 7, 8), FASTA
>6XFM_1 RNA-binding protein FUS (chains 1, 2, 3, 4, 5, 6, 7, 8)
GSYGSSSQSSSYGQPQSGSYSQQPSYGGQQQSYGQQQSYNPPQGYGQQNQYNSSSGGGGG
GGGGGNYGQDQSSMSSGGGSGGGYGNQDQSGGGGSGGYGQGDRG

Primary citation

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:

Browse structure collections

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