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Magnesium in PDB 3atf: Crystal Structure of the KIR3.2 Cytoplasmic Domain (Na+-Free Crystal Soaked in 200 Mm Cesium Chloride)

Protein crystallography data

The structure of Crystal Structure of the KIR3.2 Cytoplasmic Domain (Na+-Free Crystal Soaked in 200 Mm Cesium Chloride), PDB code: 3atf was solved by A.Inanobe, Y.Kurachi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.98 / 2.95
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 81.732, 81.732, 172.125, 90.00, 90.00, 90.00
R / Rfree (%) 22.3 / 28.1

Other elements in 3atf:

The structure of Crystal Structure of the KIR3.2 Cytoplasmic Domain (Na+-Free Crystal Soaked in 200 Mm Cesium Chloride) also contains other interesting chemical elements:

Caesium (Cs) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the KIR3.2 Cytoplasmic Domain (Na+-Free Crystal Soaked in 200 Mm Cesium Chloride) (pdb code 3atf). 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 KIR3.2 Cytoplasmic Domain (Na+-Free Crystal Soaked in 200 Mm Cesium Chloride), PDB code: 3atf:

Magnesium binding site 1 out of 1 in 3atf

Go back to Magnesium Binding Sites List in 3atf
Magnesium binding site 1 out of 1 in the Crystal Structure of the KIR3.2 Cytoplasmic Domain (Na+-Free Crystal Soaked in 200 Mm Cesium Chloride)


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 KIR3.2 Cytoplasmic Domain (Na+-Free Crystal Soaked in 200 Mm Cesium Chloride) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg382

b:33.1
occ:0.25
OE2 A:GLU236 3.9 44.5 1.0
CE A:MET313 4.2 41.2 0.5
CD A:GLU236 5.0 44.5 1.0

Reference:

A.Inanobe, A.Nakagawa, Y.Kurachi. Interactions of Cations with the Cytoplasmic Pores of Inward Rectifier K(+) Channels in the Closed State J.Biol.Chem. V. 286 41801 2011.
ISSN: ISSN 0021-9258
PubMed: 21982822
DOI: 10.1074/JBC.M111.278531
Page generated: Mon Dec 14 07:54:09 2020

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