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Alpha Synuclein fibril formed by full length protein - Rod Polymorph

Analyse Alpha Synuclein fibril formed by full length protein - Rod Polymorph in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6CU7
Type
protein
Length
600 residues
Chains
10
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
3.5
Source
Homo sapiens
Molecule
Alpha-synuclein
UniProt
P37840
Pockets
6 · best druggability 0.75

Structure

electron microscopy · resolution 3.5 · 1 distinct chain · 0% helix, 55% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
E, A, B, C, D, F, G, H, I, JAlpha-synucleinprotein600% helix, 55% strandP37840

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16320.750.8248empty
26020.730.8147empty
33200.590.7728empty
43010.550.7627empty
5630.290.7417empty

Interfaces

25 interfaces between chains.

  • G–I · 2446 Ų buried · 77 hydrogen bonds · protein-protein
  • E–C · 2431 Ų buried · 72 hydrogen bonds · protein-protein
  • F–H · 2427 Ų buried · 74 hydrogen bonds · protein-protein
  • D–F · 2425 Ų buried · 70 hydrogen bonds · protein-protein
  • H–J · 2415 Ų buried · 68 hydrogen bonds · protein-protein

Compared structures

  • 6CU7 · Alpha synuclein fibril formed by full length protein - rod polymorph · the same entry in another collection · chain J against J, TM-score 1.00
  • P37840 · AlphaFold monomer V2.0 prediction for alpha-synuclein (P37840) · a predicted model of the same protein · chain E against A, TM-score 0.28

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