› 3spi

X-ray diffraction
3.31Å resolution

Inward rectifier potassium channel Kir2.2 in complex with PIP2

Released:
DOI: 10.2210/pdb3spi/pdb
PDB entry 3spi coloured by chain, front view.
PDB entry 3spi coloured by chain, side view.
PDB entry 3spi coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Structural basis of PIP2 activation of the classical inward rectifier K+ channel Kir2.2.
Hansen SB, Tao X, MacKinnon R
Nature 477 495-8 (2011)
PMID: 21874019

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-123320 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-sensitive inward rectifier potassium channel 12 Chain: A
Molecule details ›
Chain: A
Length: 343 amino acids
Theoretical weight: 39.36 KDa
Source organism: Gallus gallus
Expression system: Komagataella pastoris
UniProt:
  • Canonical: F1NHE9 (Residues: 37-372; Coverage: 78%)
Gene name: KCNJ12
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand K 4 x K
Ligand PIO 1 x PIO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: I4
Unit cell:
a: 83.326Å b: 83.326Å c: 184.809Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.237 0.235 0.278
Expression system: Komagataella pastoris

Quick links

Citations

86 review citations

Phosphoinositides: tiny lipids with giant impact on cell regulation.
Balla T. (2013)
85 more

63 mentions without citation

Phosphoinositides regulate ion channels.
Hille et al. (2015)
62 more