› 3ffq

X-ray diffraction
2.4Å resolution

HCN2I 443-640 apo-state

Released:
DOI: 10.2210/pdb3ffq/pdb
PDB entry 3ffq coloured by chain, front view.
PDB entry 3ffq coloured by chain, side view.
PDB entry 3ffq coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Mapping the structure and conformational movements of proteins with transition metal ion FRET.
Taraska JW, Puljung MC, Olivier NB, Flynn GE, Zagotta WN
Nat Methods 6 532-7 (2009)
PMID: 19525958

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-131576 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 202 amino acids
Theoretical weight: 23.63 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: O88703 (Residues: 443-640; Coverage: 23%)
Gene names: Bcng2, Hac1, Hcn2
Sequence domains: Cyclic nucleotide-binding domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand BR 9 x BR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: I4
Unit cell:
a: 95.285Å b: 95.285Å c: 123.555Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.245 0.243 0.283
Expression system: Escherichia coli

Quick links

Citations

15 review citations

HaloTag technology: a versatile platform for biomedical applications.
England et al. (2015)
14 more

3 mentions without citation

Mapping the structure and conformational movements of proteins with transition metal ion FRET.
Taraska et al. (2009)
2 more