› 2m0q

Solution NMR

Solution NMR analysis of intact KCNE2 in detergent micelles demonstrate a straight transmembrane helix

Released:
DOI: 10.2210/pdb2m0q/pdb
PDB entry 2m0q coloured by chain, ensemble of 10 models, front view.
PDB entry 2m0q coloured by chain, ensemble of 10 models, side view.
PDB entry 2m0q coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Differential modulations of KCNQ1 by auxiliary proteins KCNE1 and KCNE2.
Li P, Liu H, Lai C, Sun P, Zeng W, Wu F, Zhang L, Wang S, Tian C, Ding J
Sci Rep 4 4973 (2014)
PMID: 24827085

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195366 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Potassium voltage-gated channel subfamily E member 2 Chain: A
Molecule details ›
Chain: A
Length: 123 amino acids
Theoretical weight: 14.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y6J6 (Residues: 1-123; Coverage: 100%)
Gene name: KCNE2
Sequence domains: Slow voltage-gated potassium channel

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 30%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Voltage-Dependent Gating: Novel Insights from KCNQ1 Channels.
Cui J. (2016)
1 more

1 mention without citation

Differential modulations of KCNQ1 by auxiliary proteins KCNE1 and KCNE2.
Li et al. (2014)