› 2l4r

Solution NMR

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

Released:
DOI: 10.2210/pdb2l4r/pdb
PDB entry 2l4r coloured by chain, ensemble of 20 models, front view.
PDB entry 2l4r coloured by chain, ensemble of 20 models, side view.
PDB entry 2l4r coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker.
Li Q, Gayen S, Chen AS, Huang Q, Raida M, Kang C
Biochem Biophys Res Commun 403 126-32 (2010)
PMID: 21055387

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171399 (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: PAS domain

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

Quick links

Citations

7 review citations

hERG K(+) channels: structure, function, and clinical significance.
Vandenberg et al. (2012)
6 more

3 mentions without citation

HERG potassium channel regulation by the N-terminal eag domain.
Gustina et al. (2012)
2 more