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Atomistry » Magnesium » PDB 5c28-5ca0 » 5c4g » |
Magnesium in PDB 5c4g: Crystal Structure of An Engineered Construct of Phosphatidylinositol 4 Kinase III Beta with the Inhibitor BQR695 in Complex with Gdp Loaded RAB11Enzymatic activity of Crystal Structure of An Engineered Construct of Phosphatidylinositol 4 Kinase III Beta with the Inhibitor BQR695 in Complex with Gdp Loaded RAB11
All present enzymatic activity of Crystal Structure of An Engineered Construct of Phosphatidylinositol 4 Kinase III Beta with the Inhibitor BQR695 in Complex with Gdp Loaded RAB11:
2.7.1.67; Protein crystallography data
The structure of Crystal Structure of An Engineered Construct of Phosphatidylinositol 4 Kinase III Beta with the Inhibitor BQR695 in Complex with Gdp Loaded RAB11, PDB code: 5c4g
was solved by
J.E.Burke,
M.L.Fowler,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of An Engineered Construct of Phosphatidylinositol 4 Kinase III Beta with the Inhibitor BQR695 in Complex with Gdp Loaded RAB11
(pdb code 5c4g). 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 An Engineered Construct of Phosphatidylinositol 4 Kinase III Beta with the Inhibitor BQR695 in Complex with Gdp Loaded RAB11, PDB code: 5c4g: Magnesium binding site 1 out of 1 in 5c4gGo back to Magnesium Binding Sites List in 5c4g
Magnesium binding site 1 out
of 1 in the Crystal Structure of An Engineered Construct of Phosphatidylinositol 4 Kinase III Beta with the Inhibitor BQR695 in Complex with Gdp Loaded RAB11
Mono view Stereo pair view
Reference:
M.L.Fowler,
J.A.Mcphail,
M.L.Jenkins,
G.R.Masson,
F.U.Rutaganira,
K.M.Shokat,
R.L.Williams,
J.E.Burke.
Using Hydrogen Deuterium Exchange Mass Spectrometry to Engineer Optimized Constructs For Crystallization of Protein Complexes: Case Study of PI4KIII Beta with RAB11. Protein Sci. V. 25 826 2016.
Page generated: Mon Dec 14 20:05:36 2020
ISSN: ESSN 1469-896X PubMed: 26756197 DOI: 10.1002/PRO.2879 |
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