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Pmca-amplified alpha-synuclein fibril polymorph, multiple system atrophy patient-derived seeds

Analyse Pmca-amplified alpha-synuclein fibril polymorph, multiple system atrophy… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7OZH
Type: protein
Length: 580 residues
Chains: 10
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-synuclein
UniProt: P37840
Pockets: 2 · best druggability 0.49

Structure

electron microscopy · 1 distinct chain · 0% helix, 41% 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, 41% strand	P37840

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	127	0.49	0.79	29	empty
2	99	0.45	0.79	23	empty

Interfaces

30 interfaces between chains.

H–J · 2190 Å² buried · 76 hydrogen bonds · protein-protein
B–D · 2190 Å² buried · 76 hydrogen bonds · protein-protein
C–E · 2187 Å² buried · 76 hydrogen bonds · protein-protein
E–G · 2186 Å² buried · 76 hydrogen bonds · protein-protein
F–H · 2186 Å² buried · 76 hydrogen bonds · protein-protein

Compared structures

7OZH · PMCA-amplified alpha-synuclein fibril polymorph, Multiple System Atrophy patient-derived… · 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 7OZH · PDBe 7OZH · UniProt P37840

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