› 4nvp

X-ray diffraction
2.5Å resolution

Structure of the cyclic nucleotide-binding domain of HCN4 channel complexed with 7-CH-cAMP

Released:
DOI: 10.2210/pdb4nvp/pdb
PDB entry 4nvp coloured by chain, front view.
PDB entry 4nvp coloured by chain, side view.
PDB entry 4nvp coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Cyclic nucleotide mapping of hyperpolarization-activated cyclic nucleotide-gated (HCN) channels.
Möller S, Alfieri A, Bertinetti D, Aquila M, Schwede F, Lolicato M, Rehmann H, Moroni A, Herberg FW
ACS Chem Biol 9 1128-37 (2014)
PMID: 24605759

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195215 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4 Chain: A
Molecule details ›
Chain: A
Length: 209 amino acids
Theoretical weight: 24.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y3Q4 (Residues: 521-723; Coverage: 17%)
Gene name: HCN4
Sequence domains: Cyclic nucleotide-binding domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 7CH 1 x 7CH
1 modified residue:
Ligand CSO 1 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P4212
Unit cell:
a: 96.01Å b: 96.01Å c: 50.17Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.198 0.27
Expression system: Escherichia coli

Quick links

Citations

6 review citations

The Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels: from Biophysics to Pharmacology of a Unique Family of Ion Channels.
Sartiani et al. (2017)
5 more

1 mention without citation

Pose Classification Using Three-Dimensional Atomic Structure-Based Neural Networks Applied to Ion Channel-Ligand Docking.
Shim et al. (2022)