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Cryo-EM structure of the N-terminally acetylated C-terminal alpha- synuclein truncation AC1-103

Analyse Cryo-EM structure of the N-terminally acetylated C-terminal alpha- synuclein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6OSM
Type
protein
Length
600 residues
Chains
10
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-synuclein
UniProt
P37840
Pockets
4 · best druggability 0.72

Structure

electron microscopy · 1 distinct chain · 0% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, JAlpha-synucleinprotein600% helix, 38% strandP37840

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12000.720.8837empty
22060.710.8839empty
32740.640.8236empty
42520.630.8131empty

Interfaces

23 interfaces between chains.

  • A–C · 2270 Ų buried · 61 hydrogen bonds · protein-protein
  • E–G · 2235 Ų buried · 50 hydrogen bonds · protein-protein
  • G–I · 2233 Ų buried · 51 hydrogen bonds · protein-protein
  • H–J · 2229 Ų buried · 50 hydrogen bonds · protein-protein
  • F–H · 2228 Ų buried · 49 hydrogen bonds · protein-protein

Compared structures

  • 6OSM · Cryo-EM structure of the N-terminally acetylated C-terminal Alpha-synuclein truncation… · the same entry in another collection · chain A against A, TM-score 1.00

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