A V-to-F substitution in SK2 channels causes CA2+ hypersensitivity and improves locomotion in a C. elegans als model

Structure

x-ray diffraction · 2 distinct chains · 62% helix, 6% strand (DSSP).

Ligands and binding sites

• 1KP · (3E)-6,7-dichloro-3-(hydroxyimino)-1,3-dihydro-2H-indol-2-one · ligand · chains B, R
• CA · Calcium ion · metal · 2 copies · chains R
• SO4 · Sulfate ion · ion · 4 copies · chains B, R
• GOL · Glycerol · additive · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Interfaces

1 interface between chains.

• B–R · 1422 Ų buried · 23 hydrogen bonds · protein-protein

Compared structures

• 6ALE · A V-to-F substitution in SK2 channels causes Ca2+ hypersensitivity and improves… · the same entry in another collection · chain B against B, TM-score 1.00
• Q9H2S1 · AlphaFold monomer V2.0 prediction for small conductance calcium- activated potassium… · a predicted model of the same protein · chain B against A, TM-score 0.66
• P0DP30 · AlphaFold monomer V2.0 prediction for calmodulin-2 (P0DP30) · a predicted model of the same protein · chain R against A, TM-score 0.51

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 Q9H2S1
• Every structure of UniProt P0DP30
• Elsewhere: RCSB PDB 6ALE · PDBe 6ALE · UniProt Q9H2S1 · UniProt P0DP30