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Atomistry » Magnesium » PDB 5xlf-5xuj » 5xlh » |
Magnesium in PDB 5xlh: Crystal Structure of Aerobically Purified and Aerobically Crystallized For 12WEEKS D. Vulgaris Miyazaki F [Nife]-HydrogenaseEnzymatic activity of Crystal Structure of Aerobically Purified and Aerobically Crystallized For 12WEEKS D. Vulgaris Miyazaki F [Nife]-Hydrogenase
All present enzymatic activity of Crystal Structure of Aerobically Purified and Aerobically Crystallized For 12WEEKS D. Vulgaris Miyazaki F [Nife]-Hydrogenase:
1.12.2.1; Protein crystallography data
The structure of Crystal Structure of Aerobically Purified and Aerobically Crystallized For 12WEEKS D. Vulgaris Miyazaki F [Nife]-Hydrogenase, PDB code: 5xlh
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 5xlh:
The structure of Crystal Structure of Aerobically Purified and Aerobically Crystallized For 12WEEKS 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 Aerobically Purified and Aerobically Crystallized For 12WEEKS D. Vulgaris Miyazaki F [Nife]-Hydrogenase
(pdb code 5xlh). 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 Aerobically Purified and Aerobically Crystallized For 12WEEKS D. Vulgaris Miyazaki F [Nife]-Hydrogenase, PDB code: 5xlh: Magnesium binding site 1 out of 1 in 5xlhGo back to Magnesium Binding Sites List in 5xlh
Magnesium binding site 1 out
of 1 in the Crystal Structure of Aerobically Purified and Aerobically Crystallized For 12WEEKS 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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