Research workbench
Type 2AB alpha-synuclein filament seeded in vitro by filaments purified from multiple systems atrophy case 1
Analyse Type 2AB alpha-synuclein filament seeded in vitro by filaments purified from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NCJ
- Type
- protein
- Length
- 774 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-synuclein
- UniProt
- P37840
- Pockets
- 7 · best druggability 0.80
Structure
electron microscopy · 2 distinct chains · 0% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Alpha-synuclein | protein | 61 | 0% helix, 69% strand | P37840 |
| G, H, I, J, K, L | Alpha-synuclein | protein | 68 | 0% helix, 32% strand | P37840 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 442 | 0.80 | 0.88 | 74 | empty |
| 2 | 175 | 0.73 | 0.90 | 58 | empty |
| 3 | 208 | 0.65 | 0.84 | 24 | empty |
| 4 | 94 | 0.41 | 0.78 | 22 | empty |
| 5 | 125 | 0.35 | 0.73 | 23 | empty |
Interfaces
27 interfaces between chains.
- H–I · 2615 Ų buried · 66 hydrogen bonds · protein-protein
- K–L · 2613 Ų buried · 61 hydrogen bonds · protein-protein
- I–J · 2607 Ų buried · 62 hydrogen bonds · protein-protein
- G–H · 2581 Ų buried · 62 hydrogen bonds · protein-protein
- J–K · 2579 Ų buried · 65 hydrogen bonds · protein-protein
Compared structures
- 7NCJ · Type 2AB alpha-synuclein filament seeded in vitro by filaments purified from Multiple… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P37840
- Elsewhere: RCSB PDB 7NCJ · PDBe 7NCJ · UniProt P37840
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