Research workbench
Structure of alpha-synuclein fibrils
Analyse Structure of alpha-synuclein fibrils in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FLT
- Type
- protein
- Length
- 580 residues
- Chains
- 10
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-synuclein
- UniProt
- P37840
- Pockets
- 4 · best druggability 0.74
Structure
electron microscopy · 1 distinct chain · 0% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J | Alpha-synuclein | protein | 58 | 0% helix, 26% strand | P37840 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 642 | 0.74 | 0.81 | 53 | empty |
| 2 | 650 | 0.73 | 0.80 | 56 | empty |
| 3 | 93 | 0.39 | 0.77 | 18 | empty |
| 4 | 77 | 0.36 | 0.76 | 18 | empty |
Interfaces
23 interfaces between chains.
- E–G · 2206 Ų buried · 64 hydrogen bonds · protein-protein
- C–E · 2200 Ų buried · 65 hydrogen bonds · protein-protein
- B–D · 2199 Ų buried · 63 hydrogen bonds · protein-protein
- F–H · 2199 Ų buried · 62 hydrogen bonds · protein-protein
- D–F · 2198 Ų buried · 62 hydrogen bonds · protein-protein
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 6FLT · PDBe 6FLT · UniProt P37840
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