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Atomistry » Magnesium » PDB 1we2-1x1s » 1wul » |
Magnesium in PDB 1wul: High Resolution Structure of the Reduced State of [Nife]Hydrogenase From Desulufovibrio Vulgaris Miyazaki FEnzymatic activity of High Resolution Structure of the Reduced State of [Nife]Hydrogenase From Desulufovibrio Vulgaris Miyazaki F
All present enzymatic activity of High Resolution Structure of the Reduced State of [Nife]Hydrogenase From Desulufovibrio Vulgaris Miyazaki F:
1.12.2.1; Protein crystallography data
The structure of High Resolution Structure of the Reduced State of [Nife]Hydrogenase From Desulufovibrio Vulgaris Miyazaki F, PDB code: 1wul
was solved by
H.Ogata,
S.Hirota,
A.Nakahara,
H.Komori,
N.Shibata,
T.Kato,
K.Kano,
Y.Higuchi,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1wul:
The structure of High Resolution Structure of the Reduced State of [Nife]Hydrogenase From Desulufovibrio Vulgaris Miyazaki F also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the High Resolution Structure of the Reduced State of [Nife]Hydrogenase From Desulufovibrio Vulgaris Miyazaki F
(pdb code 1wul). 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 High Resolution Structure of the Reduced State of [Nife]Hydrogenase From Desulufovibrio Vulgaris Miyazaki F, PDB code: 1wul: Magnesium binding site 1 out of 1 in 1wulGo back to Magnesium Binding Sites List in 1wul
Magnesium binding site 1 out
of 1 in the High Resolution Structure of the Reduced State of [Nife]Hydrogenase From Desulufovibrio Vulgaris Miyazaki F
Mono view Stereo pair view
Reference:
H.Ogata,
S.Hirota,
A.Nakahara,
H.Komori,
N.Shibata,
T.Kato,
K.Kano,
Y.Higuchi.
Activation Process of [Nife] Hydrogenase Elucidated By High-Resolution X-Ray Analyses: Conversion of the Ready to the Unready State Structure V. 13 1635 2005.
Page generated: Mon Dec 14 07:02:29 2020
ISSN: ISSN 0969-2126 PubMed: 16271886 DOI: 10.1016/J.STR.2005.07.018 |
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