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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: 5A6G
Type: protein
Length: 233 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 5.2
Source: GALLUS GALLUS
Molecule: S1-S4 domain of potassium channel subfamily T member 1; Pore domain of potassium channel…
UniProt: Q8QFV0
Pockets: 2 · best druggability 0.59

Structure

electron microscopy · resolution 5.2 · 2 distinct chains · 83% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	S1-S4 domain of potassium channel subfamily T member 1	protein	139	85% helix, 0% strand	—
B	Pore domain of potassium channel subfamily T member 1	protein	94	81% helix, 0% strand	Q8QFV0

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	156	0.59	0.83	29	empty
2	315	0.59	0.77	42	empty

Compared structures

5A6G · 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 B against A, TM-score 0.94

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 Q8QFV0
Elsewhere: RCSB PDB 5A6G · PDBe 5A6G · UniProt Q8QFV0

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