PDBe 2n7g

Solution NMR

Structure of the cyclic nucleotide-binding homology domain of the hERG channel

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Potassium voltage-gated channel subfamily H member 2 Chain: A
Molecule details ›
Chain: A
Length: 154 amino acids
Theoretical weight: 17.44 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q12809 (Residues: 734-864; Coverage: 11%)
Gene names: ERG, ERG1, HERG, KCNH2
Sequence domains: Cyclic nucleotide-binding domain
Structure domains: Jelly Rolls

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 82%
Refinement method: simulated annealing
Chemical shifts: BMR25805  
Expression system: Escherichia coli