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Potassium channel kcsa-Fab complex T75C mutant in K+

Analyse Potassium channel kcsa-Fab complex T75C mutant in K+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1S5H
Type
protein
Length
533 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Antibody Fab fragment light chain; Antibody Fab fragment heavy chain; Voltage-gated…
UniProt
Q54397
Ligands
F09, DGA, K
Pockets
5 · best druggability 0.66

Structure

x-ray diffraction · 3 distinct chains · 19% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAntibody Fab fragment light chainprotein2116% helix, 50% strand—
BAntibody Fab fragment heavy chainprotein2195% helix, 50% strand—
CVoltage-gated potassium channelprotein10374% helix, 0% strandQ54397

Ligands and binding sites

  • F09 · Nonan-1-ol · ligand · chains B, C
  • DGA · Diacyl glycerol · ligand · chains C
  • K · Potassium ion · metal · 7 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, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16960.660.7559empty
2670.550.8820empty
3730.470.8316empty
41230.460.7821empty
5760.320.7416empty

Interfaces

3 interfaces between chains.

  • A–B · 1759 Ų buried · 17 hydrogen bonds · protein-protein
  • B–C · 489 Ų buried · 8 hydrogen bonds · protein-protein
  • A–C · 438 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 1S5H · Potassium Channel Kcsa-Fab Complex T75C mutant in K+ · the same entry in another collection · chain A against A, TM-score 1.00

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