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Potassium channel kcsa-Fab complex in sodium chloride

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

PDB
2ITC
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
NA
Pockets
6 · best druggability 0.67

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
AAntibody Fab fragment heavy chainprotein2195% helix, 50% strand—
BAntibody Fab fragment light chainprotein2126% helix, 51% strand—
CVoltage-gated potassium channelprotein10375% helix, 0% strandP0A334

Ligands and binding sites

  • NA · Sodium 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17220.670.7556empty
2840.490.8317empty
3630.480.8415empty
4980.480.8121empty
51230.420.7621empty

Interfaces

3 interfaces between chains.

  • A–B · 1891 Ų buried · 16 hydrogen bonds · protein-protein
  • A–C · 504 Ų buried · 9 hydrogen bonds · protein-protein
  • B–C · 430 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 2ITC · Potassium Channel KcsA-Fab complex in Sodium Chloride · the same entry in another collection · chain A against A, TM-score 1.00

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