MolNFT v1 · #160240 · protein
Cryo-EM structure of alpha-synuclein H50Q narrow fibril
6PEO: “Cryo-EM structure of alpha-synuclein H50Q narrow fibril”. Electron microscopy, 3 pockets (best druggability 0.69). MolNFT v1 #160240 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6PEO
- Type
- protein
- Length
- 320 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-synuclein
- UniProt
- P37840
- Pockets
- 3 · best druggability 0.69
Structure
electron microscopy · 1 distinct chain · 0% helix, 78% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Alpha-synuclein | protein | 64 | 0% helix, 78% strand | P37840 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 191 | 0.69 | 0.87 | 35 | empty |
| 2 | 54 | 0.31 | 0.76 | 16 | empty |
| 3 | 70 | 0.30 | 0.74 | 15 | empty |
Interfaces
4 interfaces between chains.
- B–D · 2459 Ų buried · 82 hydrogen bonds · protein-protein
- A–B · 2456 Ų buried · 82 hydrogen bonds · protein-protein
- A–C · 2455 Ų buried · 82 hydrogen bonds · protein-protein
- C–E · 2454 Ų buried · 82 hydrogen bonds · protein-protein
Compared structures
- 6PEO · Cryo-EM structure of alpha-synuclein H50Q Narrow Fibril · 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 6PEO · PDBe 6PEO · UniProt P37840
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