MolNFT v1 · #74325 · protein
Structural basis for the camp-dependent gating in human HCN4 channel
3OTF · POTASSIUM/SODIUM hyperpolarization-activated cyclic…: “Structural basis for the camp-dependent gating in human HCN4 channel”. X-ray diffraction, 1 ligand (CMP), 2 pockets (best druggability 0.59). MolNFT v1 #74325 on GenesisL1: 3D…
- PDB
- 3OTF
- Type
- protein
- Length
- 197 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- POTASSIUM/SODIUM hyperpolarization-activated cyclic nucleotide-gated channel 4
- UniProt
- Q9Y3Q4
- Ligands
- CMP
- Pockets
- 2 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | POTASSIUM/SODIUM hyperpolarization-activated cyclic nucleotide-gated channel 4 | protein | 197 | 50% helix, 18% strand | Q9Y3Q4 |
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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 143 | 0.59 | 0.83 | 23 | CMP |
| 2 | 182 | 0.44 | 0.74 | 24 | empty |
Compared structures
- 3OTF · Structural basis for the cAMP-dependent gating in human HCN4 channel · the same entry in another collection · chain A against A, TM-score 1.00
- Q9Y3Q4 · AlphaFold monomer V2.0 prediction for POTASSIUM/SODIUM hyperpolarization-activated cyclic… · a predicted model of the same protein · chain A against A, TM-score 0.97
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9Y3Q4
- Elsewhere: RCSB PDB 3OTF · PDBe 3OTF · UniProt Q9Y3Q4
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