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MolNFT v1 · #187715 · protein

Structure of human KV1.3 (alternate conformation)

7SSY · Potassium voltage-gated channel subfamily a member 3,GREEN…: “Structure of human KV1.3 (alternate conformation)”. Electron microscopy, 1 ligand (K), 20 pockets (best druggability 0.85). MolNFT v1 #187715 on GenesisL1: 3D structure…

PDB
7SSY
Type
protein
Length
1,384 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Potassium voltage-gated channel subfamily a member 3,GREEN fluorescent protein fusion
UniProt
P22001
Ligands
K
Pockets
20 · best druggability 0.85

Structure

electron microscopy · 1 distinct chain · 63% helix, 5% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DPotassium voltage-gated channel subfamily a member 3,GREEN fluorescent protein fusionprotein34663% helix, 5% strandP22001

Ligands and binding sites

  • K · Potassium ion · metal · 3 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, 10 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111280.850.85105empty
29210.800.8240empty
33460.610.7729empty
43540.610.7634empty
53490.600.7627empty

Interfaces

6 interfaces between chains.

  • C–D · 2459 Ų buried · 21 hydrogen bonds · protein-protein
  • A–B · 2457 Ų buried · 21 hydrogen bonds · protein-protein
  • A–D · 2457 Ų buried · 21 hydrogen bonds · protein-protein
  • B–C · 2452 Ų buried · 21 hydrogen bonds · protein-protein
  • B–D · 16 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 7SSY · Structure of human Kv1.3 (alternate conformation) · the same entry in another collection · chain D against D, TM-score 1.00
  • P22001 · AlphaFold monomer V2.0 prediction for potassium voltage-gated channel subfamily a member… · a predicted model of the same protein · chain D against A, TM-score 0.93

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