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Cryo-EM structure of the SLO2.2 na-activated K channel

Analyse Cryo-EM structure of the SLO2.2 na-activated K channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5A6E
Type
protein
Length
816 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
S1-S4 domain of potassium channel subfamily T member 1; Pore domain of potassium channel…
UniProt
Q8QFV0
Pockets
16 · best druggability 0.75

Structure

electron microscopy · 4 distinct chains · 48% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AS1-S4 domain of potassium channel subfamily T member 1protein13985% helix, 0% strand—
BPore domain of potassium channel subfamily T member 1protein9481% helix, 0% strandQ8QFV0
CGating ring of potassium channel subfamily T member 1protein54031% helix, 17% strandQ8QFV0
DRCK2 elaboration of potassium channel subfamily T member 1protein4365% helix, 0% strand—

Pockets

16 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1900.750.9620empty
2510.640.9417empty
31570.590.8328empty
41700.590.8336empty
53380.590.7742empty

Interfaces

3 interfaces between chains.

  • C–D · 222 Ų buried · 0 hydrogen bonds · protein-protein
  • A–C · 60 Ų buried · 0 hydrogen bonds · protein-protein
  • B–C · 37 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 5A6E · Cryo-EM structure of the Slo2.2 Na-activated K channel · the same entry in another collection · chain A against A, TM-score 1.00
  • Q8QFV0 · AlphaFold monomer V2.0 prediction for potassium channel subfamily T member 1 (Q8QFV0) · a predicted model of the same protein · chain C against A, TM-score 0.97

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