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Structure of mutant kcsa potassium channel

Analyse Structure of mutant kcsa potassium channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1ZWI
Type
protein
Length
534 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Monoclonal antibody, heavy chain; Monoclonal antibody light chain; Voltage-gated…
UniProt
P0A334
Ligands
F09, DGA, K
Pockets
5 · best druggability 0.69

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
AMonoclonal antibody, heavy chainprotein2192% helix, 46% strand—
BMonoclonal antibody light chainprotein2127% helix, 53% strand—
CVoltage-gated potassium channelprotein10373% helix, 0% strandP0A334

Ligands and binding sites

  • F09 · Nonan-1-ol · ligand · chains A, 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, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17510.690.7659empty
22520.540.7743empty
3780.540.8615empty
4660.500.8415empty
51220.420.7621empty

Interfaces

3 interfaces between chains.

  • A–B · 1828 Ų buried · 16 hydrogen bonds · protein-protein
  • A–C · 473 Ų buried · 9 hydrogen bonds · protein-protein
  • B–C · 432 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 1ZWI · Structure of mutant KcsA potassium channel · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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