› 1n9p

X-ray diffraction
1.8Å resolution

Crystal Structure of the Cytoplasmic Domain of G-protein Activated Inward Rectifier Potassium Channel 1

Released:
DOI: 10.2210/pdb1n9p/pdb
PDB entry 1n9p coloured by chain, front view.
PDB entry 1n9p coloured by chain, side view.
PDB entry 1n9p coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structural basis of inward rectification: cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1.8 A resolution.
Nishida M, MacKinnon R
Cell 111 957-65 (2002)
PMID: 12507423

Function and Biology Details

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

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: 23.95 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P63250 (Residues: 179-371; Coverage: 39%)
Gene names: Girk1, Kcnj3
Sequence domains: Inward rectifier potassium channel C-terminal domain
Structure domains: G protein-activated inward rectifier potassium channel 1

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 8 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F2
Spacegroup: P4212
Unit cell:
a: 76.02Å b: 76.02Å c: 86.11Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.231 0.253
Expression system: Escherichia coli

Quick links

Citations

66 review citations

Inwardly rectifying potassium channels: their structure, function, and physiological roles.
Hibino et al. (2010)
65 more

17 mentions without citation

The Membrane Protein Data Bank.
Raman et al. (2006)
16 more