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Alpha-synuclein fibril from spontaneous control

Analyse Alpha-synuclein fibril from spontaneous control in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
8CYR
Type
protein
Length
864 residues
Chains
12
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
4.2
Source
Homo sapiens
Molecule
Alpha-synuclein
UniProt
P37840
Pockets
5 · best druggability 0.79

Structure

electron microscopy · resolution 4.2 · 1 distinct chain · 0% helix, 49% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, I, J, K, L, M, NAlpha-synucleinprotein720% helix, 49% strandP37840

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19330.790.8274empty
29300.780.8180empty
31940.600.8130empty
42060.570.7928empty
5540.230.7220empty

Interfaces

21 interfaces between chains.

  • K–M · 2812 Ų buried · 78 hydrogen bonds · protein-protein
  • J–L · 2810 Ų buried · 88 hydrogen bonds · protein-protein
  • A–I · 2810 Ų buried · 77 hydrogen bonds · protein-protein
  • A–E · 2809 Ų buried · 78 hydrogen bonds · protein-protein
  • C–E · 2809 Ų buried · 78 hydrogen bonds · protein-protein

Compared structures

  • P37840 · AlphaFold monomer V2.0 prediction for alpha-synuclein (P37840) · a predicted model of the same protein · chain A against A, TM-score 0.19

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