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Gadolinium in PDB 3atd: Crystal Structure of the KIR3.2 Cytoplasmic Domain (Na+-Free Crystal Soaked in 10 Mm Gadolinium Chloride and 10 Mm Magnesium Chloride)

Protein crystallography data

The structure of Crystal Structure of the KIR3.2 Cytoplasmic Domain (Na+-Free Crystal Soaked in 10 Mm Gadolinium Chloride and 10 Mm Magnesium Chloride), PDB code: 3atd 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) 48.30 / 3.01
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 82.373, 82.373, 172.810, 90.00, 90.00, 90.00
R / Rfree (%) 25.3 / 28.3

Gadolinium Binding Sites:

The binding sites of Gadolinium atom in the Crystal Structure of the KIR3.2 Cytoplasmic Domain (Na+-Free Crystal Soaked in 10 Mm Gadolinium Chloride and 10 Mm Magnesium Chloride) (pdb code 3atd). This binding sites where shown within 5.0 Angstroms radius around Gadolinium atom.
In total only one binding site of Gadolinium was determined in the Crystal Structure of the KIR3.2 Cytoplasmic Domain (Na+-Free Crystal Soaked in 10 Mm Gadolinium Chloride and 10 Mm Magnesium Chloride), PDB code: 3atd:

Gadolinium binding site 1 out of 1 in 3atd

Go back to Gadolinium Binding Sites List in 3atd
Gadolinium binding site 1 out of 1 in the Crystal Structure of the KIR3.2 Cytoplasmic Domain (Na+-Free Crystal Soaked in 10 Mm Gadolinium Chloride and 10 Mm Magnesium Chloride)


Mono view


Stereo pair view

A full contact list of Gadolinium with other atoms in the Gd binding site number 1 of Crystal Structure of the KIR3.2 Cytoplasmic Domain (Na+-Free Crystal Soaked in 10 Mm Gadolinium Chloride and 10 Mm Magnesium Chloride) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Gd1

b:0.0
occ:0.25
OE2 A:GLU236 3.4 76.3 1.0
OE1 A:GLU236 3.9 75.7 1.0
CD A:GLU236 4.1 74.5 1.0
CE A:MET313 4.2 70.8 0.5

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: Sun Dec 13 18:59:24 2020

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