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Structure of the ATP-sensitive inward rectifier potassium channel from magnetospirillum magnetotacticum

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

PDB
2WLK
Type
protein
Length
582 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ATP-sensitive inward rectifier potassium channel 10
Ligands
SPM, K, CL
Pockets
8 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BATP-sensitive inward rectifier potassium channel 10protein29127% helix, 33% strand—

Ligands and binding sites

  • SPM · Spermine · ligand · chains A, B
  • K · Potassium ion · metal · 5 copies · chains A, B
  • CL · Chloride ion · ion · chains A, B

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

Pockets

8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15220.760.8346CL
22130.580.8027empty
32280.530.7631empty
42460.500.7545empty
5830.410.7917empty

Interfaces

1 interface between chains.

  • A–B · 2492 Ų buried · 23 hydrogen bonds · protein-protein

Compared structures

  • 2WLK · Structure of the ATP-sensitive inward rectifier potassium channel from magnetospirillum… · the same entry in another collection · chain A against A, TM-score 1.00

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