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Magnesium in PDB 1yqw: Structure of the Oxidized Unready Form of Ni-Fe HydrogenaseEnzymatic activity of Structure of the Oxidized Unready Form of Ni-Fe Hydrogenase
All present enzymatic activity of Structure of the Oxidized Unready Form of Ni-Fe Hydrogenase:
1.12.2.1; Protein crystallography data
The structure of Structure of the Oxidized Unready Form of Ni-Fe Hydrogenase, PDB code: 1yqw
was solved by
A.Volbeda,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1yqw:
The structure of Structure of the Oxidized Unready Form of Ni-Fe Hydrogenase also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Structure of the Oxidized Unready Form of Ni-Fe Hydrogenase
(pdb code 1yqw). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Structure of the Oxidized Unready Form of Ni-Fe Hydrogenase, PDB code: 1yqw: Jump to Magnesium binding site number: 1; 2; 3; Magnesium binding site 1 out of 3 in 1yqwGo back to Magnesium Binding Sites List in 1yqw
Magnesium binding site 1 out
of 3 in the Structure of the Oxidized Unready Form of Ni-Fe Hydrogenase
Mono view Stereo pair view
Magnesium binding site 2 out of 3 in 1yqwGo back to Magnesium Binding Sites List in 1yqw
Magnesium binding site 2 out
of 3 in the Structure of the Oxidized Unready Form of Ni-Fe Hydrogenase
Mono view Stereo pair view
Magnesium binding site 3 out of 3 in 1yqwGo back to Magnesium Binding Sites List in 1yqw
Magnesium binding site 3 out
of 3 in the Structure of the Oxidized Unready Form of Ni-Fe Hydrogenase
Mono view Stereo pair view
Reference:
A.Volbeda,
L.Martin,
C.Cavazza,
M.Matho,
B.W.Faber,
W.Roseboom,
S.P.Albracht,
E.Garcin,
M.Rousset,
J.C.Fontecilla-Camps.
Structural Differences Between the Ready and Unready Oxidized States of [Nife] Hydrogenases. J.Biol.Inorg.Chem. V. 10 239 2005.
Page generated: Mon Dec 14 07:10:17 2020
ISSN: ISSN 0949-8257 PubMed: 15803334 DOI: 10.1007/S00775-005-0632-X |
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