› 6l1t

Electron Microscopy
3.22Å resolution

Cryo-EM structure of phosphorylated Tyr39 a-synuclein amyloid fibril

Released:
DOI: 10.2210/pdb6l1t/pdb
PDB entry 6l1t coloured by chain, front view.
PDB entry 6l1t coloured by chain, side view.
PDB entry 6l1t coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Parkinson's disease-related phosphorylation at Tyr39 rearranges α-synuclein amyloid fibril structure revealed by cryo-EM.
Zhao K, Lim YJ, Liu Z, Long H, Sun Y, Hu JJ, Zhao C, Tao Y, Zhang X, Li D, Li YM, Liu C
Proc Natl Acad Sci U S A 117 20305-20315 (2020)
PMID: 32737160
Related structures: EMD-0801

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, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 140 amino acids
Theoretical weight: 14.56 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P37840 (Residues: 1-140; Coverage: 100%)
Gene names: NACP, PARK1, SNCA
Sequence domains: Synuclein

Ligands and Environments

No bound ligands
1 modified residue:
Ligand PTR 10 x PTR

Experiments and Validation Details

Entry percentile scores
Resolution: 3.22Å
Relevant EMDB volumes: EMD-0801
Expression system: Not provided

Quick links

Citations

18 review citations

The cell biology of Parkinson's disease.
Panicker et al. (2021)
17 more

7 mentions without citation

Effects of Mutations and Post-Translational Modifications on α-Synuclein In Vitro Aggregation.
Pancoe et al. (2022)
6 more