PDBe 2l4r

Solution NMR

NMR solution structure of the N-terminal PAS domain of hERG

Released:
Source organism: Homo sapiens
Primary publication:
NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker.
Biochem. Biophys. Res. Commun. 403 126-32 (2010)
PMID: 21055387

Function and Biology Details

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: 135 amino acids
Theoretical weight: 15.3 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
Refinement method: torsion angle dynamics
Expression system: Escherichia coli