Research workbench
Heparin-remodelled alpha-synuclein fibrils
Analyse Heparin-remodelled 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
- 7V4D
- Type
- protein
- Length
- 348 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-synuclein
- UniProt
- P37840
- Pockets
- 2 · best druggability 0.50
Structure
electron microscopy · 1 distinct chain · 0% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| F, C, D, E, A, B | Alpha-synuclein | protein | 58 | 0% helix, 28% strand | P37840 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 114 | 0.50 | 0.81 | 23 | empty |
| 2 | 111 | 0.50 | 0.81 | 21 | empty |
Interfaces
9 interfaces between chains.
- C–D · 2201 Ų buried · 55 hydrogen bonds · protein-protein
- F–C · 2195 Ų buried · 55 hydrogen bonds · protein-protein
- A–B · 2191 Ų buried · 55 hydrogen bonds · protein-protein
- E–A · 2185 Ų buried · 55 hydrogen bonds · protein-protein
- C–B · 297 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7V4D · Heparin-remodelled alpha-synuclein fibrils · the same entry in another collection · chain F against F, 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 7V4D · PDBe 7V4D · UniProt P37840
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