Alpha-Synuclein with H2a-H2b dimer complex structure. Determined by X-ray diffraction at 1.72 Å resolution. Released 28 May 2025.
Explore 8ZVY in 3D Show helices and sheets RCSB PDB PDBe
8ZVY contains 18 α-helices and 8 β-strands across 2 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 |
|---|---|---|---|
| α-helix | 39-49 | 11 | |
| β-strand | 54-55 | 2 | 1 |
| α-helix | 57-84 | 28 | |
| β-strand | 89-90 | 2 | 2 |
| α-helix | 92-102 | 11 | |
| α-helix | 105-122 | 18 | |
| α-helix | 1019-1022 | 4 | |
| α-helix | 1028-1037 | 10 | |
| β-strand | 1043-1044 | 2 | 2 |
| α-helix | 1047-1073 | 27 | |
| β-strand | 1078-1079 | 2 | 1 |
| α-helix | 1081-1089 | 9 | |
| α-helix | 1092-1100 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 39-49 | 11 | |
| β-strand | 54-55 | 2 | 3 |
| α-helix | 57-82 | 26 | |
| β-strand | 89-90 | 2 | 4 |
| α-helix | 92-102 | 11 | |
| α-helix | 106-122 | 17 | |
| α-helix | 1018-1022 | 5 | |
| α-helix | 1028-1037 | 10 | |
| β-strand | 1043-1044 | 2 | 4 |
| α-helix | 1047-1073 | 27 | |
| β-strand | 1078-1079 | 2 | 3 |
| α-helix | 1081-1089 | 9 | |
| α-helix | 1092-1098 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone H2B 1.1,Histone H2A type 1 | A, B | protein | 186 | Xenopus laevis | P02281 (AlphaFold model), P06897 (AlphaFold model) |
| Isoform 1 of Alpha-synuclein | C, D | protein | 20 | Homo sapiens | P37840 (AlphaFold model) |
>8ZVY_1 Histone H2B 1.1,Histone H2A type 1 (chains A, B) GRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFERIAGEASRLAHYNKRSTITS REIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAKKAKTRSSRAGLQFPVGRVHRLLRKGN YAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLG GVTIAQ
>8ZVY_2 Isoform 1 of Alpha-synuclein (chains C, D) DNEAYEMPSEEGYQDYEPEA
Structural and functional insights into the nuclear role of Parkinson's disease-associated alpha-synuclein as a histone chaperone. Jos, S., Kambaru, A., Prasad, T.K. et al. Commun Biol (2025) 8:712-712. DOI 10.1038/s42003-025-08138-0 · PubMed
Other PDB entries of the same protein (UniProt P02281 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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