› 6l4s

Electron Microscopy
3.37Å resolution

cryo-em structure of alpha-synuclein fiber mutation type E46K

Released:
DOI: 10.2210/pdb6l4s/pdb
PDB entry 6l4s coloured by chain, front view.
PDB entry 6l4s coloured by chain, side view.
PDB entry 6l4s coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Parkinson's disease associated mutation E46K of α-synuclein triggers the formation of a distinct fibril structure.
Zhao K, Li Y, Liu Z, Long H, Zhao C, Luo F, Sun Y, Tao Y, Su XD, Li D, Li X, Liu C
Nat Commun 11 2643 (2020)
PMID: 32457390
Related structures: EMD-0833

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153511 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-synuclein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 55 amino acids
Theoretical weight: 5.4 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: P37840 (Residues: 45-99; Coverage: 39%)
Gene names: NACP, PARK1, SNCA
Sequence domains: Synuclein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.37Å
Relevant EMDB volumes: EMD-0833
Expression system: Escherichia coli K-12

Quick links

Citations

16 review citations

Biophysical processes underlying cross-seeding in amyloid aggregation and implications in amyloid pathology.
Ivanova et al. (2021)
15 more

7 mentions without citation

Relevance of Electrostatic Charges in Compactness, Aggregation, and Phase Separation of Intrinsically Disordered Proteins.
Bianchi et al. (2020)
6 more