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Electron cryo-microscopy structure of PB1-P62 type T filaments

Analyse Electron cryo-microscopy structure of PB1-P62 type T filaments in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4UF9
Type: protein
Length: 300 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sequestosome-1
UniProt: Q13501
Pockets: 2 · best druggability 0.41

Structure

electron microscopy · 1 distinct chain · 22% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, D	Sequestosome-1	protein	100	22% helix, 35% strand	Q13501

Pockets

2 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	58	0.41	0.81	17	empty
2	53	0.39	0.81	17	empty

Interfaces

1 interface between chains.

B–D · 67 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

4UF9 · Electron cryo-microscopy structure of PB1-p62 type T filaments · 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 0.83

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 Q13501
Elsewhere: RCSB PDB 4UF9 · PDBe 4UF9 · UniProt Q13501

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