› 2l1m

Solution NMR

Solution structure of the eag domain of the hERG (Kv11.1) K+ channel

Released:
DOI: 10.2210/pdb2l1m/pdb
PDB entry 2l1m coloured by chain, ensemble of 20 models, front view.
PDB entry 2l1m coloured by chain, ensemble of 20 models, side view.
PDB entry 2l1m coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Mechanistic insight into human ether-à-go-go-related gene (hERG) K+ channel deactivation gating from the solution structure of the EAG domain.
Muskett FW, Thouta S, Thomson SJ, Bowen A, Stansfeld PJ, Mitcheson JS
J Biol Chem 286 6184-91 (2011)
PMID: 21135103

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: 150 amino acids
Theoretical weight: 17.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

14 review citations

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

4 mentions without citation

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