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Cryo-EM structure of alpha-synuclein fibril polymorph 2B

Analyse Cryo-EM structure of alpha-synuclein fibril polymorph 2B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6RTB
Type
protein
Length
699 residues
Chains
10
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-synuclein
UniProt
P37840
Pockets
5 · best druggability 0.69

Structure

electron microscopy · 2 distinct chains · 0% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
H, C, I, J, E, G, B, F, AAlpha-synucleinprotein700% helix, 44% strandP37840
DAlpha-synucleinprotein690% helix, 38% strandP37840

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12420.690.8543empty
2630.340.7714empty
3760.300.7314empty
4550.280.7414empty
5530.260.7418empty

Interfaces

19 interfaces between chains.

  • D–E · 2720 Ų buried · 62 hydrogen bonds · protein-protein
  • I–J · 2701 Ų buried · 60 hydrogen bonds · protein-protein
  • C–B · 2701 Ų buried · 61 hydrogen bonds · protein-protein
  • G–F · 2697 Ų buried · 69 hydrogen bonds · protein-protein
  • H–G · 2679 Ų buried · 70 hydrogen bonds · protein-protein

Compared structures

  • 6RTB · cryo-em structure of alpha-synuclein fibril polymorph 2B · the same entry in another collection · chain H against H, TM-score 1.00

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