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Atomistry » Magnesium » PDB 6g7d-6gg6 » 6gbc » |
Magnesium in PDB 6gbc: The Structure of Variant R369A of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Amp and MolybdateEnzymatic activity of The Structure of Variant R369A of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Amp and Molybdate
All present enzymatic activity of The Structure of Variant R369A of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Amp and Molybdate:
2.10.1.1; 2.7.7.75; Protein crystallography data
The structure of The Structure of Variant R369A of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Amp and Molybdate, PDB code: 6gbc
was solved by
J.Krausze,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6gbc:
The structure of The Structure of Variant R369A of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Amp and Molybdate also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the The Structure of Variant R369A of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Amp and Molybdate
(pdb code 6gbc). 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 The Structure of Variant R369A of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Amp and Molybdate, PDB code: 6gbc: Magnesium binding site 1 out of 1 in 6gbcGo back to![]() ![]()
Magnesium binding site 1 out
of 1 in the The Structure of Variant R369A of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Amp and Molybdate
![]() Mono view ![]() Stereo pair view
Reference:
J.Krausze,
T.W.Hercher,
D.Zwerschke,
M.L.Kirk,
W.Blankenfeldt,
R.R.Mendel,
T.Kruse.
The Functional Principle of Eukaryotic Molybdenum Insertases. Biochem. J. V. 475 1739 2018.
Page generated: Tue Oct 1 01:05:43 2024
ISSN: ESSN 1470-8728 PubMed: 29717023 DOI: 10.1042/BCJ20170935 |
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