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Atomistry » Potassium » PDB 3rs9-3spj » 3spj » |
Potassium in PDB 3spj: Apo Inward Rectifier Potassium Channel KIR2.2 I223L MutantProtein crystallography data
The structure of Apo Inward Rectifier Potassium Channel KIR2.2 I223L Mutant, PDB code: 3spj
was solved by
S.B.Hansen,
X.Tao,
R.Mackinnon,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Potassium Binding Sites:
The binding sites of Potassium atom in the Apo Inward Rectifier Potassium Channel KIR2.2 I223L Mutant
(pdb code 3spj). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 5 binding sites of Potassium where determined in the Apo Inward Rectifier Potassium Channel KIR2.2 I223L Mutant, PDB code: 3spj: Jump to Potassium binding site number: 1; 2; 3; 4; 5; Potassium binding site 1 out of 5 in 3spjGo back to![]() ![]()
Potassium binding site 1 out
of 5 in the Apo Inward Rectifier Potassium Channel KIR2.2 I223L Mutant
![]() Mono view ![]() Stereo pair view
Potassium binding site 2 out of 5 in 3spjGo back to![]() ![]()
Potassium binding site 2 out
of 5 in the Apo Inward Rectifier Potassium Channel KIR2.2 I223L Mutant
![]() Mono view ![]() Stereo pair view
Potassium binding site 3 out of 5 in 3spjGo back to![]() ![]()
Potassium binding site 3 out
of 5 in the Apo Inward Rectifier Potassium Channel KIR2.2 I223L Mutant
![]() Mono view ![]() Stereo pair view
Potassium binding site 4 out of 5 in 3spjGo back to![]() ![]()
Potassium binding site 4 out
of 5 in the Apo Inward Rectifier Potassium Channel KIR2.2 I223L Mutant
![]() Mono view ![]() Stereo pair view
Potassium binding site 5 out of 5 in 3spjGo back to![]() ![]()
Potassium binding site 5 out
of 5 in the Apo Inward Rectifier Potassium Channel KIR2.2 I223L Mutant
![]() Mono view ![]() Stereo pair view
Reference:
S.B.Hansen,
X.Tao,
R.Mackinnon.
Structural Basis of Pip(2) Activation of the Classical Inward Rectifier K(+) Channel KIR2.2. Nature V. 477 495 2011.
Page generated: Mon Aug 12 09:31:12 2024
ISSN: ISSN 0028-0836 PubMed: 21874019 DOI: 10.1038/NATURE10370 |
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