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Tetramerization dynamics of the C-terminus underlies isoform-specific camp-gating in hcn channels

Analyse Tetramerization dynamics of the C-terminus underlies isoform-specific… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3U10
Type
protein
Length
202 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
POTASSIUM/SODIUM hyperpolarization-activated cyclic nucleotide-gated channel 2
UniProt
Q9UL51
Ligands
CMP
Pockets
2 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APOTASSIUM/SODIUM hyperpolarization-activated cyclic nucleotide-gated channel 2protein20249% helix, 19% strandQ9UL51

Ligands and binding sites

  • CMP · Adenosine-3',5'-cyclic-monophosphate · ligand · chains A

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11120.700.9221CMP
22660.500.7428empty

Compared structures

  • 3U10 · Tetramerization dynamics of the C-terminus underlies isoform-specific cAMP-gating in HCN… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9UL51 · AlphaFold monomer V2.0 prediction for POTASSIUM/SODIUM hyperpolarization-activated cyclic… · a predicted model of the same protein · chain A against A, TM-score 0.96

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