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Structure of alpha-synuclein fibrils

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

PDB: 6H6B
Type: protein
Length: 580 residues
Chains: 10
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-synuclein
UniProt: P37840
Pockets: 5 · best druggability 0.74

Structure

electron microscopy · 1 distinct chain · 0% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J	Alpha-synuclein	protein	58	0% helix, 47% strand	P37840

Pockets

5 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	577	0.74	0.82	49	empty
2	571	0.74	0.82	49	empty
3	116	0.42	0.76	18	empty
4	123	0.42	0.76	18	empty
5	55	0.25	0.73	22	empty

Interfaces

23 interfaces between chains.

A–H · 2179 Å² buried · 65 hydrogen bonds · protein-protein
B–C · 2175 Å² buried · 63 hydrogen bonds · protein-protein
A–B · 2173 Å² buried · 62 hydrogen bonds · protein-protein
E–J · 2172 Å² buried · 61 hydrogen bonds · protein-protein
I–J · 2170 Å² buried · 61 hydrogen bonds · protein-protein

Compared structures

6H6B · Structure of alpha-synuclein fibrils · 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 6H6B · PDBe 6H6B · UniProt P37840

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