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Human KV4.2-KCHIP2 channel complex in an open state, transmembrane region

Analyse Human KV4.2-KCHIP2 channel complex in an open state, transmembrane region in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7UK5
Type
protein
Length
1,036 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Potassium voltage-gated channel subfamily D member 2
UniProt
Q9NZV8
Ligands
K
Pockets
12 · best druggability 0.82

Structure

electron microscopy · 1 distinct chain · 74% helix, 1% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DPotassium voltage-gated channel subfamily D member 2protein25974% helix, 1% strandQ9NZV8

Ligands and binding sites

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

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18370.820.8441empty
26900.680.7557empty
37120.680.7559empty
46570.670.7660empty
56900.670.7557empty

Interfaces

6 interfaces between chains.

  • A–B · 1574 Ų buried · 6 hydrogen bonds · protein-protein
  • B–C · 1573 Ų buried · 6 hydrogen bonds · protein-protein
  • A–D · 1569 Ų buried · 6 hydrogen bonds · protein-protein
  • C–D · 1566 Ų buried · 6 hydrogen bonds · protein-protein
  • A–C · 51 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 7UK5 · Human Kv4.2-KChIP2 channel complex in an open state, transmembrane region · the same entry in another collection · chain D against D, TM-score 1.00
  • Q9NZV8 · AlphaFold monomer V2.0 prediction for potassium voltage-gated channel subfamily D member… · a predicted model of the same protein · chain A against A, TM-score 0.94

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