Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2
Homo sapiens
State in the Current Structure
| Assembly | Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Associated Components | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|
| 1 | Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count | Chain A； UniProt 521–672 | Fragment：cyclic nucleotide binding domain (UNP residues 521-672) | No other associated polymer | SOLUTION NMR NMR measurement conditions：pH 7；298 K；Pressure ambient NMR sample composition：1 mM [U-15N] HCN2 CNBD, 20 mM potassium phosphate, 150 mM potassium chloride, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition：1 mM [U-13C; U-15N] HCN2 CNBD, 20 mM potassium phosphate, 150 mM potassium chloride, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition：1 mM HCN2 CNBD, 20 mM potassium phosphate, 150 mM potassium chloride, 90% H2O/10% D2O | 90% H2O/10% D2O | Resolution not provided |
Other States of the Same Protein in the Database
Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.
2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | HCN2_HUMAN |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 7–158； UniProt 521–672 |
