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Cryo-EM structure of P62-PB1 filament (S-type)

Analyse Cryo-EM structure of P62-PB1 filament (S-type) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6TH3
Type
protein
Length
312 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Sequestosome-1
UniProt
Q13501
Pockets
1 · best druggability 0.34

Structure

electron microscopy · 1 distinct chain · 18% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CSequestosome-1protein10418% helix, 31% strandQ13501

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1550.340.7811empty

Interfaces

2 interfaces between chains.

  • A–C · 129 Ų buried · 3 hydrogen bonds · protein-protein
  • A–B · 68 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 6TH3 · Cryo-EM structure of p62-PB1 filament (S-type) · the same entry in another collection · chain A against A, TM-score 1.00
  • Q13501 · AlphaFold monomer V2.0 prediction for sequestosome-1 (Q13501) · a predicted model of the same protein · chain A against A, TM-score 0.95

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