› 6pes

Electron Microscopy
3.6Å resolution

Cryo-EM structure of alpha-synuclein H50Q Wide Fibril

Released:
DOI: 10.2210/pdb6pes/pdb
PDB entry 6pes coloured by chain, front view.
PDB entry 6pes coloured by chain, side view.
PDB entry 6pes coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of fibrils formed by α-synuclein hereditary disease mutant H50Q reveal new polymorphs.
Boyer DR, Li B, Sun C, Fan W, Sawaya MR, Jiang L, Eisenberg DS
Nat Struct Mol Biol 26 1044-1052 (2019)
PMID: 31695184
Related structures: EMD-20331

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153502 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-synuclein Chains: A, B, C, D, E, V, W, X, Y, Z
Molecule details ›
Chains: A, B, C, D, E, V, W, X, Y, Z
Length: 140 amino acids
Theoretical weight: 14.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P37840 (Residues: 1-140; Coverage: 100%)
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: 3.6Å
Relevant EMDB volumes: EMD-20331
Expression system: Escherichia coli

Quick links

Citations

26 review citations

Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis.
Nguyen et al. (2021)
25 more

6 mentions without citation

Neuropathology and molecular diagnosis of Synucleinopathies.
Koga et al. (2021)
5 more