› 5xrr

X-ray diffraction
1.5Å resolution

Crystal structure of FUS (54-59) SYSSYG

Released:
DOI: 10.2210/pdb5xrr/pdb
PDB entry 5xrr coloured by chain, front view.
PDB entry 5xrr coloured by chain, side view.
PDB entry 5xrr coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Atomic structures of FUS LC domain segments reveal bases for reversible amyloid fibril formation.
Luo F, Gui X, Zhou H, Gu J, Li Y, Liu X, Zhao M, Li D, Li X, Liu C
Nat Struct Mol Biol 25 341-346 (2018)
PMID: 29610493

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-152977 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNA-binding protein FUS Chain: A
Molecule details ›
Chain: A
Length: 6 amino acids
Theoretical weight: 663 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P35637 (Residues: 54-59; Coverage: 1%)
Gene names: FUS, TLS

Ligands and Environments

1 bound ligand:
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U1
Spacegroup: P21212
Unit cell:
a: 28.24Å b: 30.27Å c: 4.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.204 0.241
Expression system: Not provided

Quick links

Citations

35 review citations

The molecular language of membraneless organelles.
Gomes et al. (2019)
34 more

2 mentions without citation

Side Chain Hydrogen-Bonding Interactions within Amyloid-like Fibrils Formed by the Low-Complexity Domain of FUS: Evidence from Solid State Nuclear Magnetic Resonance Spectroscopy.
Murray et al. (2020)
1 more