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Type 1B alpha-synuclein filament seeded in vitro by filaments purified from multiple systems atrophy case 1

Analyse Type 1B alpha-synuclein filament seeded in vitro by filaments purified from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7NCH
Type
protein
Length
816 residues
Chains
12
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-synuclein
UniProt
P37840
Pockets
10 · best druggability 0.77

Structure

electron microscopy · 1 distinct chain · 0% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, LAlpha-synucleinprotein680% helix, 41% strandP37840

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12550.770.9158empty
22590.760.9059empty
33970.590.7547empty
43190.580.7740empty
5780.510.8430empty

Interfaces

30 interfaces between chains.

  • K–L · 2653 Ų buried · 52 hydrogen bonds · protein-protein
  • E–F · 2653 Ų buried · 51 hydrogen bonds · protein-protein
  • C–D · 2636 Ų buried · 62 hydrogen bonds · protein-protein
  • D–E · 2623 Ų buried · 61 hydrogen bonds · protein-protein
  • B–C · 2622 Ų buried · 67 hydrogen bonds · protein-protein

Compared structures

  • 7NCH · Type 1B alpha-synuclein filament seeded in vitro by filaments purified from Multiple… · the same entry in another collection · chain E against E, TM-score 1.00

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