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Kcsa T75G mutant in the nonconductive state

Analyse Kcsa T75G mutant in the nonconductive state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5EBM
Type
protein
Length
531 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Antibody Fab fragment light chain; PH-gated potassium channel kcsa
UniProt
P0A334
Ligands
DGA, F09, K
Pockets
6 · best druggability 0.69

Structure

x-ray diffraction · 3 distinct chains · 18% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAntibody Fab fragment light chainprotein2184% helix, 51% strand—
BAntibody Fab fragment light chainprotein2126% helix, 53% strand—
CPH-gated potassium channel kcsaprotein10172% helix, 0% strandP0A334

Ligands and binding sites

  • DGA · Diacyl glycerol · ligand · chains C
  • F09 · Nonan-1-ol · ligand · chains A, C
  • K · Potassium ion · metal · 3 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, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17070.690.7754empty
2750.500.8516empty
3610.490.8516empty
41330.470.7829empty
51430.460.7734empty

Interfaces

3 interfaces between chains.

  • A–B · 1799 Ų buried · 15 hydrogen bonds · protein-protein
  • A–C · 480 Ų buried · 10 hydrogen bonds · protein-protein
  • B–C · 435 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 5EBM · KcsA T75G mutant in the nonconductive state · the same entry in another collection · chain A against A, TM-score 1.00

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