GL1X · GenesisL1 explorer

MolNFT v1 · #187224 · protein

Human katp channel in open conformation, focused on kir (C166S G334D double mutant) and sur TMD0

7S5T · ATP-sensitive inward rectifier potassium channel 11: “Human katp channel in open conformation, focused on kir (C166S G334D double mutant) and sur TMD0”. Electron microscopy, 1 ligand (K), 16 pockets (best druggability 0.87). MolNFT…

PDB
7S5T
Type
protein
Length
1,284 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ATP-sensitive inward rectifier potassium channel 11
UniProt
B2RC52
Ligands
K
Pockets
16 · best druggability 0.87

Structure

electron microscopy · 1 distinct chain · 31% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DATP-sensitive inward rectifier potassium channel 11protein32131% helix, 29% strandB2RC52

Ligands and binding sites

  • K · Potassium ion · metal · 2 copies · chains A, B, C, D

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

Pockets

16 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16620.870.9281empty
22310.660.8442empty
32400.640.8242empty
42370.630.8244empty
53790.630.7850empty

Interfaces

6 interfaces between chains.

  • B–C · 3424 Ų buried · 32 hydrogen bonds · protein-protein
  • C–D · 3423 Ų buried · 33 hydrogen bonds · protein-protein
  • A–D · 3421 Ų buried · 32 hydrogen bonds · protein-protein
  • A–B · 3401 Ų buried · 31 hydrogen bonds · protein-protein
  • A–C · 43 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 7S5T · Human KATP channel in open conformation, focused on Kir (C166S G334D double mutant) and… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.