Structure of human KCNQ4-ML213 complex with PIP2

Structure

electron microscopy · 2 distinct chains.

Ligands and binding sites

• PT5 · (1S)-2-{[(R)-hydroxy{[(1r,2r,3s,4r,5r,6s)-2,3,6-trihydroxy-4,5-bis(phosphonooxy) cyclohexyl]oxy}phosphoryl]oxy}-1-[(octadecanoyloxy) methyl]ethyl (8E,11E)-icosa-5,8,11,14-tetraenoate · ligand · 8 copies · chains A, C, E, G
• 7YV · (1S,2S,4R)-N-(2,4,6-trimethylphenyl) bicyclo[2.2.1]heptane-2-carboxamid · ligand · 4 copies · chains A, C, G, E
• K · Potassium ion · metal · 4 copies · chains A, C, E, G

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

Compared structures

• 7VNP · Structure of human KCNQ4-ML213 complex with PIP2 · the same entry in another collection · chain H against H, TM-score 1.00
• P56696 · AlphaFold monomer V2.0 prediction for potassium voltage-gated channel subfamily kqt… · a predicted model of the same protein · chain A against A, TM-score 0.78
• P0DP25 · AlphaFold monomer V2.0 prediction for calmodulin-3 (P0DP25) · a predicted model of the same protein · chain H against A, TM-score 0.43

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 P56696
• Every structure of UniProt A0A140NCD0
• Every structure of UniProt P0DP25
• Elsewhere: RCSB PDB 7VNP · PDBe 7VNP · UniProt P56696 · UniProt A0A140NCD0 · UniProt P0DP25