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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
5A6F
Type
protein
Length
583 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Gating ring of potassium channel subfamily T member 1; RCK2 elaboration of potassium…
UniProt
Q8QFV0
Pockets
11 · best druggability 0.77

Structure

electron microscopy · 2 distinct chains · 34% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
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

11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11070.770.9627empty
23920.630.7853empty
3510.580.9117empty
4650.540.8722empty
5520.530.8816empty

Interfaces

1 interface between chains.

  • C–D · 223 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 5A6F · Cryo-EM structure of the Slo2.2 Na-activated K channel · the same entry in another collection · chain C against C, 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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