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Structure of a pancreatic ATP-sensitive potassium channel

Analyse Structure of a pancreatic ATP-sensitive potassium channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5WUA
Type
protein
Length
6,540 residues
Chains
8
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ATP-sensitive inward rectifier potassium channel 11, superfolder GFP; SUR1
UniProt
Q61743
Pockets
20 · best druggability 0.84

Structure

electron microscopy · 2 distinct chains · 56% helix, 9% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DATP-sensitive inward rectifier potassium channel 11, superfolder GFPprotein32328% helix, 19% strandQ61743
E, F, G, HSUR1protein131263% helix, 6% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19050.840.86110empty
23870.830.9139empty
38800.820.84125empty
47130.800.8493empty
58350.800.83111empty

Interfaces

14 interfaces between chains.

  • A–B · 3301 Ų buried · 14 hydrogen bonds · protein-protein
  • C–D · 3243 Ų buried · 12 hydrogen bonds · protein-protein
  • B–C · 3225 Ų buried · 12 hydrogen bonds · protein-protein
  • A–D · 3135 Ų buried · 10 hydrogen bonds · protein-protein
  • B–F · 575 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 5WUA · Structure of a Pancreatic ATP-sensitive Potassium Channel · the same entry in another collection · chain H against H, TM-score 1.00
  • Q61743 · 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 0.94

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