Research workbench
Cryo-EM structure of the N-terminal alpha-synuclein truncation 41-140
Analyse Cryo-EM structure of the N-terminal alpha-synuclein truncation 41-140 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LC9
- Type
- protein
- Length
- 525 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-synuclein
- UniProt
- P37840
- Pockets
- 1 · best druggability 0.61
Structure
electron microscopy · 3 distinct chains · 0% helix, 70% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| F, H, I, J, K | Alpha-synuclein | protein | 38 | 0% helix, 74% strand | P37840 |
| A, B, C, D, E, G | Alpha-synuclein | protein | 51 | 0% helix, 63% strand | P37840 |
| L | Alpha-synuclein | protein | 29 | 0% helix, 79% strand | P37840 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.61 | 0.90 | 27 | empty |
Interfaces
37 interfaces between chains.
- B–C · 2095 Ų buried · 63 hydrogen bonds · protein-protein
- C–D · 2085 Ų buried · 70 hydrogen bonds · protein-protein
- A–B · 2084 Ų buried · 64 hydrogen bonds · protein-protein
- D–E · 2075 Ų buried · 67 hydrogen bonds · protein-protein
- E–G · 2069 Ų buried · 58 hydrogen bonds · protein-protein
Compared structures
- 7LC9 · Cryo-EM structure of the N-terminal alpha-synuclein truncation 41-140 · the same entry in another collection · chain J against J, 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 7LC9 · PDBe 7LC9 · UniProt P37840
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