2N0A: Alpha-synuclein
Atomic-resolution structure of alpha-synuclein fibrils. Determined by solid-state NMR. Released 23 Mar 2016.
- Method
- Solid-state NMR
- Organism
- Homo sapiens
- Chains
- 10
- Atoms
- 10,130
- Mol. weight
- 144.76 kDa
- Released
- 23 Mar 2016
Explore 2N0A in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2N0A contains 13 α-helices and 70 β-strands across 10 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.
Chain A: 5 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-7 | 3 | |
| α-helix | 17-19 | 3 | |
| α-helix | 26-27 | 2 | |
| β-strand | 30 | 1 | 1 |
| β-strand | 35 | 1 | 2 |
| β-strand | 38-55 | 18 | 3 |
| β-strand | 61-66 | 6 | 4 |
| β-strand | 70-78 | 9 | 5 |
| β-strand | 81-83 | 3 | 6 |
| β-strand | 88-97 | 10 | 7 |
| α-helix | 107-112 | 6 | |
| α-helix | 128-132 | 5 | |
Chain B: 1 helix, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-13 | 2 | |
| β-strand | 30 | 1 | 1 |
| β-strand | 35 | 1 | 2 |
| β-strand | 38-55 | 18 | 3 |
| β-strand | 61-66 | 6 | 4 |
| β-strand | 70-78 | 9 | 5 |
| β-strand | 81-83 | 3 | 6 |
| β-strand | 88-97 | 10 | 7 |
Chain C: 2 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 13-15 | 3 | |
| β-strand | 30 | 1 | 1 |
| β-strand | 35 | 1 | 2 |
| β-strand | 38-55 | 18 | 3 |
| β-strand | 61-66 | 6 | 4 |
| β-strand | 70-78 | 9 | 5 |
| β-strand | 81-83 | 3 | 6 |
| β-strand | 88-97 | 10 | 7 |
| α-helix | 112-114 | 3 | |
Chain D: 1 helix, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 30 | 1 | 1 |
| β-strand | 35 | 1 | 2 |
| β-strand | 38-55 | 18 | 3 |
| β-strand | 61-66 | 6 | 4 |
| β-strand | 70-78 | 9 | 5 |
| β-strand | 81-83 | 3 | 6 |
| β-strand | 88-97 | 10 | 7 |
| α-helix | 127-129 | 3 | |
Chain E: 1 helix, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 30 | 1 | 1 |
| β-strand | 35 | 1 | 2 |
| β-strand | 38-55 | 18 | 3 |
| β-strand | 61-66 | 6 | 4 |
| β-strand | 70-78 | 9 | 5 |
| β-strand | 81-83 | 3 | 6 |
| β-strand | 88-97 | 10 | 7 |
| α-helix | 107-109 | 3 | |
Chain F: 0 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 28-30 | 3 | 1 |
| β-strand | 35 | 1 | 2 |
| β-strand | 38-55 | 18 | 3 |
| β-strand | 61-66 | 6 | 4 |
| β-strand | 70-78 | 9 | 5 |
| β-strand | 81-83 | 3 | 6 |
| β-strand | 88-97 | 10 | 7 |
Chain G: 1 helix, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 28-30 | 3 | 1 |
| β-strand | 35 | 1 | 2 |
| β-strand | 38-55 | 18 | 3 |
| β-strand | 61-66 | 6 | 4 |
| β-strand | 70-78 | 9 | 5 |
| β-strand | 81-83 | 3 | 6 |
| β-strand | 88-97 | 10 | 7 |
| α-helix | 123-125 | 3 | |
Chain H: 0 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 29-30 | 2 | 1 |
| β-strand | 35 | 1 | 2 |
| β-strand | 38-55 | 18 | 3 |
| β-strand | 61-66 | 6 | 4 |
| β-strand | 70-78 | 9 | 5 |
| β-strand | 81-83 | 3 | 6 |
| β-strand | 88-98 | 11 | 7 |
2 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Alpha-synuclein | A, B, C, D, E, F, G, H, I, J | protein | 140 | Homo sapiens | P37840 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J), FASTA
>2N0A_1 Alpha-synuclein (chains A, B, C, D, E, F, G, H, I, J)
MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTK
EQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDP
DNEAYEMPSEEGYQDYEPEA
Primary citation
Solid-state NMR structure of a pathogenic fibril of full-length human alpha-synuclein. Tuttle, M.D., Comellas, G., Nieuwkoop, A.J. et al. Nat Struct Mol Biol (2016) 23:409-415. DOI 10.1038/nsmb.3194 · PubMed
Other PDB entries of the same protein (UniProt P37840 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 8JJV 1.23 Å, Structure of truncated form of nanobody in complex with alpha-synuclein peptide
- 8JLY 1.29 Å, Structure of nanobody in complex with alpha-synuclein peptide
- 3Q27 1.3 Å, Cyrstal structure of human alpha-synuclein (32-57) fused to maltose binding protein (MBP)
- 4R0U 1.38 Å, Tgvtava, an amyloid forming segment from alpha synuclein, residues 72-78
- 6I42 1.38 Å, Structure of the alpha-Synuclein PreNAC/Cyclophilin A-complex
- 4ZNN 1.41 Å, MicroED structure of the segment, GVVHGVTTVA, from the A53T familial mutant of…
- 4RIL 1.43 Å, Structure of the amyloid forming segment, GAVVTGVTAVA, from the NAC domain of…
- 4R0W 1.5 Å, Vvtgvta, an amyloid forming segment from alpha synuclein, residues 70-76
- 3Q26 1.54 Å, Cyrstal structure of human alpha-synuclein (10-42) fused to maltose binding protein (MBP)
- 3Q28 1.6 Å, Cyrstal structure of human alpha-synuclein (58-79) fused to maltose binding protein (MBP)
- 5CRW 1.6 Å, Crystal structure of the b'-a' domain of oxidized protein disulfide isomerase complexed…
- 2X6M 1.62 Å, Structure of a single domain camelid antibody fragment in complex with a C-terminal…
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