Research workbench
Cryo-EM structure of the N-terminally acetylated C-terminal alpha- synuclein truncation AC1-122
Analyse Cryo-EM structure of the N-terminally acetylated C-terminal alpha- synuclein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6OSL
- Type
- protein
- Length
- 590 residues
- Chains
- 10
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-synuclein
- UniProt
- P37840
- Pockets
- 6 · best druggability 0.75
Structure
electron microscopy · 1 distinct chain · 0% helix, 59% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J | Alpha-synuclein | protein | 59 | 0% helix, 59% strand | P37840 |
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 631 | 0.75 | 0.82 | 48 | empty |
| 2 | 621 | 0.75 | 0.82 | 47 | empty |
| 3 | 101 | 0.55 | 0.84 | 27 | empty |
| 4 | 89 | 0.53 | 0.85 | 25 | empty |
| 5 | 70 | 0.27 | 0.72 | 17 | empty |
Interfaces
17 interfaces between chains.
- F–H · 2219 Ų buried · 74 hydrogen bonds · protein-protein
- B–D · 2213 Ų buried · 74 hydrogen bonds · protein-protein
- G–I · 2202 Ų buried · 72 hydrogen bonds · protein-protein
- E–G · 2200 Ų buried · 74 hydrogen bonds · protein-protein
- D–F · 2200 Ų buried · 70 hydrogen bonds · protein-protein
Compared structures
- 6OSL · Cryo-EM structure of the N-terminally acetylated C-terminal Alpha-synuclein truncation… · the same entry in another collection · chain D against D, 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 6OSL · PDBe 6OSL · UniProt P37840
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