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On the structural basis of modal gating behavior in K+CHANNELS - E71I

Analyse On the structural basis of modal gating behavior in K+CHANNELS - E71I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3OR7
Type
protein
Length
534 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Antibody Fab fragment heavy chain; Antibody Fab fragment light chain; Voltage-gated…
UniProt
P0A334
Ligands
K
Pockets
5 · best druggability 0.68

Structure

x-ray diffraction · 3 distinct chains · 18% helix, 40% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAntibody Fab fragment heavy chainprotein2194% helix, 48% strand—
BAntibody Fab fragment light chainprotein2126% helix, 50% strand—
CVoltage-gated potassium channelprotein10373% helix, 0% strandP0A334

Ligands and binding sites

  • K · Potassium ion · metal · 5 copies · chains C

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

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17360.680.7666empty
2630.590.9017empty
31610.540.8031empty
4600.530.8716empty
5920.370.7514empty

Interfaces

3 interfaces between chains.

  • A–B · 1836 Ų buried · 18 hydrogen bonds · protein-protein
  • A–C · 499 Ų buried · 10 hydrogen bonds · protein-protein
  • B–C · 431 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 3OR7 · On the structural basis of modal gating behavior in K+channels - E71I · the same entry in another collection · chain A against A, TM-score 1.00

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