MolNFT v1 · #155351 · protein
Cryo-EM structure of alpha-synuclein fiber mutation type E46K
6L4S: “Cryo-EM structure of alpha-synuclein fiber mutation type E46K”. Electron microscopy, 2 pockets (best druggability 0.49). MolNFT v1 #155351 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6L4S
- Type
- protein
- Length
- 330 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-synuclein
- UniProt
- P37840
- Pockets
- 2 · best druggability 0.49
Structure
electron microscopy · 1 distinct chain · 0% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Alpha-synuclein | protein | 55 | 0% helix, 35% strand | P37840 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 132 | 0.49 | 0.79 | 23 | empty |
| 2 | 129 | 0.47 | 0.79 | 24 | empty |
Interfaces
11 interfaces between chains.
- B–F · 2287 Ų buried · 57 hydrogen bonds · protein-protein
- A–E · 2271 Ų buried · 54 hydrogen bonds · protein-protein
- B–D · 2259 Ų buried · 54 hydrogen bonds · protein-protein
- A–C · 2254 Ų buried · 56 hydrogen bonds · protein-protein
- C–D · 294 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6L4S · cryo-em structure of alpha-synuclein fiber mutation type E46K · 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 6L4S · PDBe 6L4S · UniProt P37840
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