› 7lc9

Electron Microscopy
3.2Å resolution

Cryo-EM structure of the N-terminal alpha-synuclein truncation 41-140

Released:
DOI: 10.2210/pdb7lc9/pdb
PDB entry 7lc9 coloured by chain, front view.
PDB entry 7lc9 coloured by chain, side view.
PDB entry 7lc9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The N terminus of α-synuclein dictates fibril formation.
McGlinchey RP, Ni X, Shadish JA, Jiang J, Lee JC
Proc Natl Acad Sci U S A 118 (2021)
PMID: 34452994
Related structures: EMD-23270

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153504 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-synuclein Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 100 amino acids
Theoretical weight: 10.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P37840 (Residues: 41-140; Coverage: 71%)
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: 3.2Å
Relevant EMDB volumes: EMD-23270
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Pathological and Therapeutic Advances in Parkinson's Disease: Mitochondria in the Interplay.
Naren et al. (2023)
5 more

3 mentions without citation

Structures of α-synuclein filaments from human brains with Lewy pathology.
Yang et al. (2022)
2 more