Cryo-EM structure of in-vitro alpha-synuclein fibril. Determined by electron microscopy at 2.04 Å resolution. Released 24 Jul 2024.
Explore 9CK3 in 3D Show helices and sheets RCSB PDB PDBe
9CK3 contains 0 α-helices and 72 β-strands across 12 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 16-21 | 6 | 1 |
| β-strand | 37-57 | 21 | 2 |
| β-strand | 60-66 | 7 | 3 |
| β-strand | 69-82 | 14 | 4 |
| β-strand | 86-92 | 7 | 5 |
| β-strand | 95-96 | 2 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Alpha-synuclein | A, B, C, D, E, F, G, H, I, J, K, L | protein | 140 | Homo sapiens | P37840 (AlphaFold model) |
>9CK3_1 Alpha-synuclein (chains A, B, C, D, E, F, G, H, I, J, K, L) MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTK EQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDP DNEAYEMPSEEGYQDYEPEA
High-resolution Cryo-EM Structure Determination of a-Synuclein-A Prototypical Amyloid Fibril. Sanchez, J.C., Pierson, J.A., Borcik, C.G. et al. Bio Protoc (2025) 15:e5171-e5171. DOI 10.21769/BioProtoc.5171 · PubMed
Other PDB entries of the same protein (UniProt P37840 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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