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Atomistry » Magnesium » PDB 1t5t-1tkd » 1t5t | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 1t5t-1tkd » 1t5t » |
Magnesium in PDB 1t5t: Structure of the (Sr)CA2+-Atpase CA2-E1-Adp:ALF4- FormEnzymatic activity of Structure of the (Sr)CA2+-Atpase CA2-E1-Adp:ALF4- Form
All present enzymatic activity of Structure of the (Sr)CA2+-Atpase CA2-E1-Adp:ALF4- Form:
3.6.3.8; Protein crystallography data
The structure of Structure of the (Sr)CA2+-Atpase CA2-E1-Adp:ALF4- Form, PDB code: 1t5t
was solved by
T.L.-M.Sorensen,
J.V.Moller,
P.Nissen,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1t5t:
The structure of Structure of the (Sr)CA2+-Atpase CA2-E1-Adp:ALF4- Form also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Structure of the (Sr)CA2+-Atpase CA2-E1-Adp:ALF4- Form
(pdb code 1t5t). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of the (Sr)CA2+-Atpase CA2-E1-Adp:ALF4- Form, PDB code: 1t5t: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 1t5tGo back to Magnesium Binding Sites List in 1t5t
Magnesium binding site 1 out
of 2 in the Structure of the (Sr)CA2+-Atpase CA2-E1-Adp:ALF4- Form
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 1t5tGo back to Magnesium Binding Sites List in 1t5t
Magnesium binding site 2 out
of 2 in the Structure of the (Sr)CA2+-Atpase CA2-E1-Adp:ALF4- Form
Mono view Stereo pair view
Reference:
T.L.Sorensen,
J.V.Moller,
P.Nissen.
Phosphoryl Transfer and Calcium Ion Occlusion in the Calcium Pump. Science V. 304 1672 2004.
Page generated: Tue Aug 13 14:28:12 2024
ISSN: ISSN 0036-8075 PubMed: 15192230 DOI: 10.1126/SCIENCE.1099366 |
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