PDBe 2l0w

Solution NMR

Solution NMR structure of the N-terminal PAS domain of HERG potassium 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: 138 amino acids
Theoretical weight: 15.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q12809 (Residues: 1-135; Coverage: 12%)
Gene names: ERG, ERG1, HERG, KCNH2
Sequence domains: PAS domain
Structure domains: Beta-Lactamase

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 84%
Refinement method: DGSA-distance geometry simulated annealing, Generalised Born Energy Minimization, GENERALISED BORN ENERGY MINIMIZATION WITH NMR RESTRAINTS
Chemical shifts: BMR17066  
Expression system: Escherichia coli