Table 2:

K_ATP channel cryoEM structures

Constructs	Ligands (PDB/ EMDB ID; resolution)	Structure highlights	Reference
hamster SUR1 (Q608K)+mouse Kir6.2	Glibenclamide (5WUA/EMD-6689; 5.6Å)	Kir6.2 closed and SUR1 inward-facing Glibenclamide and PIP2 density tentatively assigned; however, glibenclamide density assignment was later corrected in Wu et al.	[65]
hamsterSUR1+ratKir6.2	Glibenclamide+ATP (5TWV/5.8Å)	Resolved ATP cryoEM density in Kir6.2	[67]
hamsterSUR1+ratKir6.2	Glibenclamide+ATP (6BAA/EMD-7073; 3.7Å)	Resolved glibenclamide cryoEM density in SUR1	[66]
humanSUR1-(6aa linker)-humanKir6.2 fusion1	MgATP+PIP2 Class 1: quatrefoil (6C3O/EMD-7339; 3.9Å) Class 2: propeller (6C3P/EMD-7338; 5.6Å)	SUR1’s NBDs dimerized, with MgATP bound at NBD1 and MgADP at NBD2; Kir6.2 closed, bound to ATP Two conformations were resolved: quatrefoil and propeller, with the quatrefoil form being the dominant class	[64]
hamsterSUR1-(39aa linker)-mouseKir6.2 fusion1	ATPγS (5YW8/EM D-6848; 4.4Å) Glibenclamide/ATPγS (5YKE/EMD-6831; 4.1Å) MgADP/NN414/PIP2 (5YWC/EMD-6852; 4.3Å)	Glibenclamide density assigned Only propeller-like conformation was observed in MgADP bound, NBDs-dimerized structure Tentative assignment of NN414 density	[68]
hamsterSUR1-(39aa linker)-mouseKir6.2 fusion	Repaglinide+ATPγS (6JB1/EMD-9787; 3.3Å)	Repaglinide density assigned	[63]
hamsterSUR1+ratKir6.2	SUR1 bound to: Glibenclamide+ATP	SUR1 NBD1 bound to ATP in all structures except the apo state structure	[52]
	(6PZA/EM D-20530; 3.7Å) Repaglinide+ATP (6PZ9/EMD-20528; 3.7Å) Carbamazepine+ATP (6PZC/EMD-20530; 4.3Å) ATP only (6PZI/EMD-20535; 4.5Å) Apo (6PZB/EMD-20533; 4.6Å)	Glibenclamide, repaglinide, and carbamazepine cryoEM density found in the same binding pocket, and no density observed in the pocket in ATP only or apo state structures Kir6.2 N-term density assigned in the drug-bound structures

¹Only the dominant class or the best resolution structure for each liganded state is included.