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Magnesium in PDB 3agw: Crystal Structure of the Cytoplasmic Domain of G-Protein-Gated Inward Rectifier Potassium Channel KIR3.2 in the Absence of Na+

Protein crystallography data

The structure of Crystal Structure of the Cytoplasmic Domain of G-Protein-Gated Inward Rectifier Potassium Channel KIR3.2 in the Absence of Na+, PDB code: 3agw was solved by A.Inanobe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.73 / 2.20
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 81.943, 81.943, 172.769, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 23.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Cytoplasmic Domain of G-Protein-Gated Inward Rectifier Potassium Channel KIR3.2 in the Absence of Na+ (pdb code 3agw). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of the Cytoplasmic Domain of G-Protein-Gated Inward Rectifier Potassium Channel KIR3.2 in the Absence of Na+, PDB code: 3agw:

Magnesium binding site 1 out of 1 in 3agw

Go back to Magnesium Binding Sites List in 3agw
Magnesium binding site 1 out of 1 in the Crystal Structure of the Cytoplasmic Domain of G-Protein-Gated Inward Rectifier Potassium Channel KIR3.2 in the Absence of Na+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Cytoplasmic Domain of G-Protein-Gated Inward Rectifier Potassium Channel KIR3.2 in the Absence of Na+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1

b:68.6
occ:0.25
OE2 A:GLU236 4.4 64.2 1.0
CE A:MET313 4.6 48.8 0.5
OE1 A:GLU236 4.7 57.9 1.0
CD A:GLU236 5.0 61.4 1.0

Reference:

A.Inanobe, A.Nakagawa, T.Matsuura, Y.Kurachi. A Structural Determinant For the Control of PIP2 Sensitivity in G Protein-Gated Inward Rectifier K+ Channels J.Biol.Chem. V. 285 38517 2010.
ISSN: ISSN 0021-9258
PubMed: 20880843
DOI: 10.1074/JBC.M110.161703
Page generated: Mon Dec 14 07:53:13 2020

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