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The electron crystallography structure of the camp-bound potassium channel MLOK1

Analyse The electron crystallography structure of the camp-bound potassium channel MLOK1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4CHV
Type
protein
Length
1,372 residues
Chains
4
Method
electron crystallography
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cyclic nucleotide-gated potassium channel MLL3241
UniProt
Q98GN8
Ligands
K
Pockets
20 · best druggability 0.84

Structure

electron crystallography · 1 distinct chain · 64% helix, 9% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DCyclic nucleotide-gated potassium channel MLL3241protein34364% helix, 9% strandQ98GN8

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

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19910.840.85102empty
210000.800.81105empty
311110.780.79114empty
47580.770.8165empty
58450.760.8079empty

Interfaces

6 interfaces between chains.

  • A–B · 2519 Ų buried · 33 hydrogen bonds · protein-protein
  • B–C · 2504 Ų buried · 29 hydrogen bonds · protein-protein
  • A–D · 2493 Ų buried · 30 hydrogen bonds · protein-protein
  • C–D · 2470 Ų buried · 30 hydrogen bonds · protein-protein
  • A–C · 167 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 4CHV · The electron crystallography structure of the cAMP-bound potassium channel MloK1 · the same entry in another collection · chain D against D, TM-score 1.00
  • Q98GN8 · AlphaFold monomer V2.0 prediction for cyclic nucleotide-gated potassium channel MLL3241… · a predicted model of the same protein · chain D against A, TM-score 0.69

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