GL1X · GenesisL1 explorer

MolNFT v1 · #19690 · protein

Structure of a voltage-dependent K+ channel beta subunit

1QRQ · Protein (kv BETA2 protein): “Structure of a voltage-dependent K+ channel beta subunit”. X-ray diffraction, 1 ligand (NDP), 15 pockets (best druggability 0.82). MolNFT v1 #19690 on GenesisL1: 3D structure, binding sites and pockets…

PDB
1QRQ
Type
protein
Length
1,300 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein (kv BETA2 protein)
UniProt
P62483
Ligands
NDP
Pockets
15 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DProtein (kv BETA2 protein)protein32550% helix, 17% strandP62483

Ligands and binding sites

  • NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 4 copies · chains A, B, C, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18000.820.8541empty
22240.780.9240NDP
32320.760.9041NDP
43050.750.8755NDP
53190.740.8661NDP

Interfaces

4 interfaces between chains.

  • A–C · 965 Ų buried · 23 hydrogen bonds · protein-protein
  • B–C · 959 Ų buried · 23 hydrogen bonds · protein-protein
  • B–D · 958 Ų buried · 22 hydrogen bonds · protein-protein
  • A–D · 948 Ų buried · 22 hydrogen bonds · protein-protein

Compared structures

  • 1QRQ · Structure of a voltage-dependent K+ channel beta subunit · the same entry in another collection · chain A against A, TM-score 1.00
  • P62483 · AlphaFold monomer V2.0 prediction for voltage-gated potassium channel subunit beta-2… · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.