MolNFT v1 · #174626 · protein

Cryo-EM structure of the HE46K cross-seeded hwt alpha-synuclein fibril

7C1D: “Cryo-EM structure of the HE46K cross-seeded hwt alpha-synuclein fibril”. Electron microscopy, 3 pockets (best druggability 0.38). MolNFT v1 #174626 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7C1D
Type: protein
Length: 306 residues
Chains: 6
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-synuclein
UniProt: P37840
Pockets: 3 · best druggability 0.38

Structure

electron microscopy · 1 distinct chain · 0% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E, A, B, F, C, D	Alpha-synuclein	protein	51	0% helix, 12% strand	P37840

Pockets

3 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	99	0.38	0.75	18	empty
2	90	0.35	0.74	16	empty
3	51	0.32	0.78	22	empty

Interfaces

9 interfaces between chains.

E–A · 1817 Å² buried · 37 hydrogen bonds · protein-protein
F–C · 1815 Å² buried · 36 hydrogen bonds · protein-protein
C–D · 1805 Å² buried · 36 hydrogen bonds · protein-protein
A–B · 1795 Å² buried · 36 hydrogen bonds · protein-protein
A–C · 179 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

7C1D · Cryo-EM structure of the hE46K cross-seeded hWT alpha-synuclein fibril · 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 7C1D · PDBe 7C1D · UniProt P37840

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