Cryo-EM structure of human katp bound to ATP and ADP in propeller form

Structure

electron microscopy · 2 distinct chains · 57% helix, 11% strand (DSSP).

Ligands and binding sites

• ATP · Adenosine-5'-triphosphate · ligand · 8 copies · chains A, B, D, C, E, H, G, F
• ADP · Adenosine-5'-diphosphate · ligand · 4 copies · chains E, H, G, F
• MG · Magnesium ion · metal · 8 copies · chains E, H, G, F

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Interfaces

14 interfaces between chains.

• A–D · 3138 Ų buried · 25 hydrogen bonds · protein-protein
• B–C · 3129 Ų buried · 24 hydrogen bonds · protein-protein
• A–B · 3112 Ų buried · 23 hydrogen bonds · protein-protein
• D–C · 3108 Ų buried · 20 hydrogen bonds · protein-protein
• C–G · 1073 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

• 6C3P · Cryo-EM structure of human KATP bound to ATP and ADP in propeller form · the same entry in another collection · chain F against F, TM-score 1.00
• Q14654 · AlphaFold monomer V2.0 prediction for ATP-sensitive inward rectifier potassium channel 11… · a predicted model of the same protein · chain A against A, TM-score 0.98
• Q09428 · AlphaFold monomer V2.0 prediction for ATP-binding cassette sub-family C member 8 (Q09428) · a predicted model of the same protein · chain H against A, TM-score 0.87

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 Q14654
• Every structure of UniProt Q09428
• Elsewhere: RCSB PDB 6C3P · PDBe 6C3P · UniProt Q14654 · UniProt Q09428