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Molecular structure of fus low sequence complexity domain protein fibrils

Analyse Molecular structure of fus low sequence complexity domain protein fibrils in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5W3N
Type
protein
Length
549 residues
Chains
9
Method
solid-state nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
RNA-binding protein fus
UniProt
P35637
Pockets
1 · best druggability 0.40

Structure

solid-state nmr · 1 distinct chain · 0% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, IRNA-binding protein fusprotein610% helix, 33% strandP35637

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1860.400.7728empty

Interfaces

15 interfaces between chains.

  • E–F · 2325 Ų buried · 90 hydrogen bonds · protein-protein
  • D–E · 2322 Ų buried · 90 hydrogen bonds · protein-protein
  • F–G · 2322 Ų buried · 91 hydrogen bonds · protein-protein
  • G–H · 2320 Ų buried · 91 hydrogen bonds · protein-protein
  • C–D · 2320 Ų buried · 91 hydrogen bonds · protein-protein

Compared structures

  • 5W3N · Molecular structure of FUS low sequence complexity domain protein fibrils · the same entry in another collection · chain I against I, TM-score 1.00
  • P35637 · AlphaFold monomer V2.0 prediction for RNA-binding protein fus (P35637) · a predicted model of the same protein · chain I against A, TM-score 0.30

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