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Atomistry » Magnesium » PDB 5xlg-5xus » 5xlg » |
Magnesium in PDB 5xlg: Crystal Structure of Anaerobically Purified and Aerobically Crystallized D. Vulgaris Miyazaki F [Nife]-HydrogenaseEnzymatic activity of Crystal Structure of Anaerobically Purified and Aerobically Crystallized D. Vulgaris Miyazaki F [Nife]-Hydrogenase
All present enzymatic activity of Crystal Structure of Anaerobically Purified and Aerobically Crystallized D. Vulgaris Miyazaki F [Nife]-Hydrogenase:
1.12.2.1; Protein crystallography data
The structure of Crystal Structure of Anaerobically Purified and Aerobically Crystallized D. Vulgaris Miyazaki F [Nife]-Hydrogenase, PDB code: 5xlg
was solved by
K.Nishikawa,
S.Mochida,
T.Hiromoto,
N.Shibata,
Y.Higuchi,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5xlg:
The structure of Crystal Structure of Anaerobically Purified and Aerobically Crystallized D. Vulgaris Miyazaki F [Nife]-Hydrogenase also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Anaerobically Purified and Aerobically Crystallized D. Vulgaris Miyazaki F [Nife]-Hydrogenase
(pdb code 5xlg). 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 Anaerobically Purified and Aerobically Crystallized D. Vulgaris Miyazaki F [Nife]-Hydrogenase, PDB code: 5xlg: Magnesium binding site 1 out of 1 in 5xlgGo back to![]() ![]()
Magnesium binding site 1 out
of 1 in the Crystal Structure of Anaerobically Purified and Aerobically Crystallized D. Vulgaris Miyazaki F [Nife]-Hydrogenase
![]() Mono view ![]() Stereo pair view
Reference:
K.Nishikawa,
S.Mochida,
T.Hiromoto,
N.Shibata,
Y.Higuchi.
Ni-Elimination From the Active Site of the Standard [Nife]‐Hydrogenase Upon Oxidation By O2. J. Inorg. Biochem. V. 177 435 2017.
Page generated: Mon Sep 30 09:34:19 2024
ISSN: ISSN 1873-3344 PubMed: 28967475 DOI: 10.1016/J.JINORGBIO.2017.09.011 |
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