› 3k6n

X-ray diffraction
2Å resolution

Crystal structure of the S225E mutant Kir3.1 cytoplasmic pore domain

Released:
DOI: 10.2210/pdb3k6n/pdb
PDB entry 3k6n coloured by chain, front view.
PDB entry 3k6n coloured by chain, side view.
PDB entry 3k6n coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Physical determinants of strong voltage sensitivity of K(+) channel block.
Xu Y, Shin HG, Szép S, Lu Z
Nat Struct Mol Biol 16 1252-8 (2009)
PMID: 19915587

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159063 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
G protein-activated inward rectifier potassium channel 1 Chain: A
Molecule details ›
Chain: A
Length: 207 amino acids
Theoretical weight: 23.62 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P63250 (Residues: 41-371; Coverage: 41%)
Gene names: Girk1, Kcnj3
Sequence domains:
Structure domains: G protein-activated inward rectifier potassium channel 1

Ligands and Environments

1 bound ligand:
Ligand NA 5 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P4212
Unit cell:
a: 77.455Å b: 77.455Å c: 86.723Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.254 0.254 0.266
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Emerging roles for G protein-gated inwardly rectifying potassium (GIRK) channels in health and disease.
Lüscher et al. (2010)
4 more

4 mentions without citation

Cholesterol sensitivity of KIR2.1 is controlled by a belt of residues around the cytosolic pore.
Rosenhouse-Dantsker et al. (2011)
3 more