Research workbench
Structure of the cyclic nucleotide-binding domain of HCN4 channel complexed with 7-ch-camp
Analyse Structure of the cyclic nucleotide-binding domain of HCN4 channel complexed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NVP
- Type
- protein
- Length
- 201 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
- 7CH
- Pockets
- 2 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | POTASSIUM/SODIUM hyperpolarization-activated cyclic nucleotide-gated channel 4 | protein | 201 | 51% helix, 20% strand | Q9Y3Q4 |
Ligands and binding sites
- 7CH · (2S,4aR,6R,7R,7aS)-6-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)tetrahydro-4H-furo[3,2-d][1,3,2]dioxaphosphinine-2,7-diol 2-oxide · 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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 127 | 0.69 | 0.90 | 23 | 7CH |
| 2 | 227 | 0.51 | 0.76 | 26 | empty |
Modifications
Observed in the structure: 1 modified (oxidation).
Compared structures
- 4NVP · Structure of the cyclic nucleotide-binding domain of HCN4 channel complexed with 7-CH-cAMP · 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 4NVP · PDBe 4NVP · UniProt Q9Y3Q4
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