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Crystal structure of a voltage-gated K+ channel pore domain in a closed state in lipid membranes

Analyse Crystal structure of a voltage-gated K+ channel pore domain in a closed state… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4H37
Type
protein
Length
172 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
LMO2059 protein
UniProt
Q8Y5K1
Ligands
K
Pockets
1 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 74% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BLMO2059 proteinprotein8674% helix, 0% strandQ8Y5K1

Ligands and binding sites

  • K · Potassium ion · metal · 4 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1980.360.7415empty

Interfaces

1 interface between chains.

  • A–B · 903 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 4H37 · Crystal structure of a voltage-gated K+ channel pore domain in a closed state in lipid… · the same entry in another collection · chain A against A, TM-score 1.00

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