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mouse alpha-synuclein

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

PDB: 9EWV
Type: protein
Length: 768 residues
Chains: 12
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.9
Source: Mus musculus
Molecule: Alpha-synuclein
UniProt: O55042
Pockets: 7 · best druggability 0.76

Structure

electron microscopy · resolution 2.9 · 1 distinct chain · 0% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, I, F, G, H, J, K, L	Alpha-synuclein	protein	64	0% helix, 55% strand	O55042

Pockets

7 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	312	0.76	0.88	42	empty
2	312	0.75	0.87	42	empty
3	143	0.71	0.91	24	empty
4	117	0.68	0.91	43	empty
5	112	0.66	0.90	42	empty

Interfaces

21 interfaces between chains.

A–B · 2468 Å² buried · 67 hydrogen bonds · protein-protein
F–G · 2468 Å² buried · 68 hydrogen bonds · protein-protein
H–J · 2466 Å² buried · 67 hydrogen bonds · protein-protein
B–C · 2465 Å² buried · 66 hydrogen bonds · protein-protein
C–D · 2464 Å² buried · 68 hydrogen bonds · protein-protein

Compared structures

O55042 · AlphaFold monomer V2.0 prediction for alpha-synuclein (O55042) · a predicted model of the same protein · chain A against A, TM-score 0.24

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 O55042
Elsewhere: RCSB PDB 9EWV · PDBe 9EWV · UniProt O55042

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