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Alpha synuclein fibril formed by full length protein - twister polymorph

Analyse Alpha synuclein fibril formed by full length protein - twister polymorph in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6CU8
Type: protein
Length: 410 residues
Chains: 10
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-synuclein
UniProt: P37840
Pockets: 4 · best druggability 0.71

Structure

electron microscopy · 1 distinct chain · 0% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E, A, B, C, D, F, G, H, I, J	Alpha-synuclein	protein	41	0% helix, 32% strand	P37840

Pockets

4 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	266	0.71	0.86	40	empty
2	250	0.65	0.83	41	empty
3	263	0.56	0.77	31	empty
4	274	0.53	0.75	34	empty

Interfaces

23 interfaces between chains.

E–G · 1886 Å² buried · 49 hydrogen bonds · protein-protein
B–D · 1875 Å² buried · 49 hydrogen bonds · protein-protein
A–C · 1871 Å² buried · 48 hydrogen bonds · protein-protein
H–J · 1868 Å² buried · 48 hydrogen bonds · protein-protein
F–H · 1863 Å² buried · 45 hydrogen bonds · protein-protein

Compared structures

6CU8 · Alpha Synuclein fibril formed by full length protein - Twister Polymorph · the same entry in another collection · chain E against E, 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 6CU8 · PDBe 6CU8 · UniProt P37840

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