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Cryo-EM structure of alpha-synuclein fiber

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

PDB: 6A6B
Type: protein
Length: 756 residues
Chains: 12
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-synuclein
UniProt: P37840
Pockets: 8 · best druggability 0.76

Structure

electron microscopy · 1 distinct chain · 0% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L	Alpha-synuclein	protein	63	0% helix, 40% strand	P37840

Pockets

8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	372	0.76	0.87	52	empty
2	363	0.75	0.86	52	empty
3	211	0.49	0.76	28	empty
4	242	0.46	0.73	31	empty
5	104	0.33	0.72	19	empty

Interfaces

21 interfaces between chains.

I–J · 2479 Å² buried · 73 hydrogen bonds · protein-protein
K–L · 2459 Å² buried · 68 hydrogen bonds · protein-protein
D–E · 2459 Å² buried · 69 hydrogen bonds · protein-protein
G–H · 2449 Å² buried · 67 hydrogen bonds · protein-protein
H–I · 2444 Å² buried · 68 hydrogen bonds · protein-protein

Compared structures

6A6B · cryo-em structure of alpha-synuclein fiber · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P37840
Elsewhere: RCSB PDB 6A6B · PDBe 6A6B · UniProt P37840

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