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Cryo-EM structure of amyloid fibril formed by fus low complexity domain

Analyse Cryo-EM structure of amyloid fibril formed by fus low complexity domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7VQQ
Type: protein
Length: 273 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fusion protein of mcerulean and fus lcd
UniProt: P35637
Pockets: 2 · best druggability 0.55

Structure

electron microscopy · 1 distinct chain · 0% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Fusion protein of mcerulean and fus lcd	protein	91	0% helix, 21% strand	P35637

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	101	0.55	0.83	17	empty
2	175	0.50	0.77	24	empty

Interfaces

2 interfaces between chains.

A–B · 3426 Å² buried · 77 hydrogen bonds · protein-protein
B–C · 3402 Å² buried · 69 hydrogen bonds · protein-protein

Compared structures

7VQQ · Cryo-EM structure of amyloid fibril formed by FUS low complexity domain · the same entry in another collection · chain A against A, TM-score 1.00
P35637 · AlphaFold monomer V2.0 prediction for RNA-binding protein fus (P35637) · a predicted model of the same protein · chain A against A, TM-score 0.21

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 P35637
Elsewhere: RCSB PDB 7VQQ · PDBe 7VQQ · UniProt P35637

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