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Atomistry » Magnesium » PDB 6g6z-6gfu » 6gal » |
Magnesium in PDB 6gal: Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q Collected at pH 10Enzymatic activity of Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q Collected at pH 10
All present enzymatic activity of Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q Collected at pH 10:
1.12.99.6; Protein crystallography data
The structure of Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q Collected at pH 10, PDB code: 6gal
was solved by
S.B.Carr,
F.A.Armstrong,
R.M.Evans,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6gal:
The structure of Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q Collected at pH 10 also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q Collected at pH 10
(pdb code 6gal). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q Collected at pH 10, PDB code: 6gal: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 6galGo back to Magnesium Binding Sites List in 6gal
Magnesium binding site 1 out
of 2 in the Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q Collected at pH 10
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 6galGo back to Magnesium Binding Sites List in 6gal
Magnesium binding site 2 out
of 2 in the Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q Collected at pH 10
Mono view Stereo pair view
Reference:
R.M.Evans,
P.A.Ash,
S.E.Beaton,
E.J.Brooke,
K.A.Vincent,
S.B.Carr,
F.A.Armstrong.
Mechanistic Exploitation of A Self-Repairing, Blocked Proton Transfer Pathway in An O2-Tolerant [Nife]-Hydrogenase. J. Am. Chem. Soc. V. 140 10208 2018.
Page generated: Tue Oct 1 01:03:23 2024
ISSN: ESSN 1520-5126 PubMed: 30070475 DOI: 10.1021/JACS.8B04798 |
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