GL1X · GenesisL1 explorer

Research workbench

Kcsa potassium channel in the open-inactivated state with 32 a opening at T112

Analyse Kcsa potassium channel in the open-inactivated state with 32 a opening at T112 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3F5W
Type
protein
Length
519 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Antibody heavy chain; Antibody light chain; Voltage-gated potassium channel
UniProt
P0A334
Ligands
K
Pockets
6 · best druggability 0.69

Structure

x-ray diffraction · 3 distinct chains · 16% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAntibody heavy chainprotein2195% helix, 51% strand—
BAntibody light chainprotein2126% helix, 51% strand—
CVoltage-gated potassium channelprotein8868% helix, 0% strandP0A334

Ligands and binding sites

  • K · Potassium ion · metal · 2 copies · chains C

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

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17660.690.7659empty
2660.600.9115empty
31700.530.7936empty
4500.470.8619empty
5780.470.8218empty

Interfaces

3 interfaces between chains.

  • A–B · 1859 Ų buried · 17 hydrogen bonds · protein-protein
  • A–C · 488 Ų buried · 11 hydrogen bonds · protein-protein
  • B–C · 402 Ų buried · 9 hydrogen bonds · protein-protein

Compared structures

  • 3F5W · KcsA Potassium channel in the open-inactivated state with 32 A opening at T112 · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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