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Atomistry » Magnesium » PDB 6q5a-6qin » 6qgt | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 6q5a-6qin » 6qgt » |
Magnesium in PDB 6qgt: The Carbon Monoxide Inhibition of F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina BarkeriEnzymatic activity of The Carbon Monoxide Inhibition of F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri
All present enzymatic activity of The Carbon Monoxide Inhibition of F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri:
1.12.98.1; Protein crystallography data
The structure of The Carbon Monoxide Inhibition of F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri, PDB code: 6qgt
was solved by
Y.Ilina,
C.Lorent,
S.Katz,
J.H.Jeoung,
S.Shima,
M.Horch,
I.Zebger,
H.Dobbek,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6qgt:
The structure of The Carbon Monoxide Inhibition of F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the The Carbon Monoxide Inhibition of F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri
(pdb code 6qgt). 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 Carbon Monoxide Inhibition of F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri, PDB code: 6qgt: Magnesium binding site 1 out of 1 in 6qgtGo back to Magnesium Binding Sites List in 6qgt
Magnesium binding site 1 out
of 1 in the The Carbon Monoxide Inhibition of F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri
Mono view Stereo pair view
Reference:
Y.Ilina,
C.Lorent,
S.Katz,
J.H.Jeoung,
S.Shima,
M.Horch,
I.Zebger,
H.Dobbek.
X-Ray Crystallography and Vibrational Spectroscopy Reveal the Key Determinants of Biocatalytic Dihydrogen Cycling By [Nife] Hydrogenases. Angew.Chem.Int.Ed.Engl. 2019.
Page generated: Tue Oct 1 15:28:24 2024
ISSN: ESSN 1521-3773 PubMed: 31591784 DOI: 10.1002/ANIE.201908258 |
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