Potassium in PDB 3syp: Crystal Structure of the G Protein-Gated Inward Rectifier K+ Channel GIRK2 (KIR3.2) R201A Mutant

The structure of Crystal Structure of the G Protein-Gated Inward Rectifier K+ Channel GIRK2 (KIR3.2) R201A Mutant, PDB code: 3syp was solved by M.R.Whorton, R.Mackinnon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.36 / 3.12
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	85.431, 85.431, 178.209, 90.00, 90.00, 90.00
R / Rfree (%)	26.2 / 29.6

The binding sites of Potassium atom in the Crystal Structure of the G Protein-Gated Inward Rectifier K+ Channel GIRK2 (KIR3.2) R201A Mutant (pdb code 3syp). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 5 binding sites of Potassium where determined in the Crystal Structure of the G Protein-Gated Inward Rectifier K+ Channel GIRK2 (KIR3.2) R201A Mutant, PDB code: 3syp:
Jump to Potassium binding site number: 1; 2; 3; 4; 5;

Potassium binding site 1 out of 5 in the Crystal Structure of the G Protein-Gated Inward Rectifier K+ Channel GIRK2 (KIR3.2) R201A Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of the G Protein-Gated Inward Rectifier K+ Channel GIRK2 (KIR3.2) R201A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:K501 b:0.6 occ:0.13 K A:K502 2.9 0.8 0.1 O A:GLY156 3.5 0.3 1.0 O A:TYR157 3.7 0.5 1.0 C A:TYR157 4.1 0.2 1.0 C A:GLY156 4.6 0.5 1.0 CA A:TYR157 4.7 0.1 1.0 N A:GLY158 4.7 0.1 1.0 CA A:GLY158 5.0 0.3 1.0

Potassium binding site 2 out of 5 in the Crystal Structure of the G Protein-Gated Inward Rectifier K+ Channel GIRK2 (KIR3.2) R201A Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of the G Protein-Gated Inward Rectifier K+ Channel GIRK2 (KIR3.2) R201A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:K502 b:0.8 occ:0.13 K A:K503 2.9 0.8 0.1 K A:K501 2.9 0.6 0.1 O A:ILE155 3.1 0.4 1.0 O A:GLY156 3.5 0.3 1.0 C A:ILE155 4.4 0.3 1.0 C A:GLY156 4.4 0.5 1.0

Potassium binding site 3 out of 5 in the Crystal Structure of the G Protein-Gated Inward Rectifier K+ Channel GIRK2 (KIR3.2) R201A Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Crystal Structure of the G Protein-Gated Inward Rectifier K+ Channel GIRK2 (KIR3.2) R201A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:K503 b:0.8 occ:0.13 K A:K502 2.9 0.8 0.1 O A:THR154 3.2 0.5 1.0 K A:K504 3.2 0.5 0.1 O A:ILE155 3.2 0.4 1.0 C A:ILE155 4.1 0.3 1.0 C A:THR154 4.3 0.5 1.0 CA A:ILE155 4.4 0.6 1.0 N A:ILE155 4.9 0.5 1.0

Potassium binding site 4 out of 5 in the Crystal Structure of the G Protein-Gated Inward Rectifier K+ Channel GIRK2 (KIR3.2) R201A Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Crystal Structure of the G Protein-Gated Inward Rectifier K+ Channel GIRK2 (KIR3.2) R201A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:K504 b:0.5 occ:0.13 OG1 A:THR154 3.2 0.2 1.0 K A:K503 3.2 0.8 0.1 O A:THR154 3.3 0.5 1.0 C A:THR154 4.2 0.5 1.0 CB A:THR154 4.3 0.2 1.0 O A:THR153 4.5 0.0 1.0 CA A:THR154 4.9 0.6 1.0

Potassium binding site 5 out of 5 in the Crystal Structure of the G Protein-Gated Inward Rectifier K+ Channel GIRK2 (KIR3.2) R201A Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 5 of Crystal Structure of the G Protein-Gated Inward Rectifier K+ Channel GIRK2 (KIR3.2) R201A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:K505 b:0.2 occ:1.00 O A:TYR266 4.4 67.2 1.0 CE2 A:TYR266 4.4 66.9 1.0 CZ A:TYR266 4.6 67.5 1.0 CD1 A:TYR267 4.6 69.1 1.0 CD2 A:TYR266 4.6 64.5 1.0 CE1 A:TYR266 4.9 65.8 1.0 OH A:TYR266 4.9 70.0 1.0 CA A:TYR267 4.9 66.0 1.0 CG A:TYR266 5.0 63.2 1.0

M.R.Whorton, R.Mackinnon. Crystal Structure of the Mammalian GIRK2 K(+) Channel and Gating Regulation By G Proteins, Pip(2), and Sodium. Cell(Cambridge,Mass.) V. 147 199 2011.
ISSN: ISSN 0092-8674
PubMed: 21962516
DOI: 10.1016/J.CELL.2011.07.046