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Alpha-synuclein fibrils

Analyse 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: 7L7H
Type: protein
Length: 352 residues
Chains: 8
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-synuclein
UniProt: P37840
Pockets: 5 · best druggability 0.66

Structure

electron microscopy · 1 distinct chain · 0% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H	Alpha-synuclein	protein	44	0% helix, 14% strand	P37840

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	636	0.66	0.75	62	empty
2	607	0.64	0.75	60	empty
3	188	0.63	0.84	36	empty
4	136	0.56	0.82	36	empty
5	83	0.50	0.83	16	empty

Interfaces

13 interfaces between chains.

B–C · 1708 Å² buried · 37 hydrogen bonds · protein-protein
E–F · 1683 Å² buried · 34 hydrogen bonds · protein-protein
C–D · 1678 Å² buried · 33 hydrogen bonds · protein-protein
F–G · 1659 Å² buried · 31 hydrogen bonds · protein-protein
G–H · 1658 Å² buried · 39 hydrogen bonds · protein-protein

Compared structures

7L7H · 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 7L7H · PDBe 7L7H · UniProt P37840

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