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Atomistry » Magnesium » PDB 6q5a-6qin » 6qgr | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 6q5a-6qin » 6qgr » |
Magnesium in PDB 6qgr: The F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri at the Nia-S StateEnzymatic activity of The F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri at the Nia-S State
All present enzymatic activity of The F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri at the Nia-S State:
1.12.98.1; Protein crystallography data
The structure of The F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri at the Nia-S State, PDB code: 6qgr
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 6qgr:
The structure of The F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri at the Nia-S State also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the The F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri at the Nia-S State
(pdb code 6qgr). 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 F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri at the Nia-S State, PDB code: 6qgr: Magnesium binding site 1 out of 1 in 6qgrGo back to Magnesium Binding Sites List in 6qgr
Magnesium binding site 1 out
of 1 in the The F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri at the Nia-S State
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 15:28:14 2024
ISSN: ESSN 1521-3773 PubMed: 31591784 DOI: 10.1002/ANIE.201908258 |
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