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Atomistry » Calcium » PDB 1spu-1t5s » 1t5s | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 1spu-1t5s » 1t5s » |
Calcium in PDB 1t5s: Structure of the (Sr)CA2+-Atpase CA2-E1-Amppcp FormEnzymatic activity of Structure of the (Sr)CA2+-Atpase CA2-E1-Amppcp Form
All present enzymatic activity of Structure of the (Sr)CA2+-Atpase CA2-E1-Amppcp Form:
3.6.3.8; Protein crystallography data
The structure of Structure of the (Sr)CA2+-Atpase CA2-E1-Amppcp Form, PDB code: 1t5s
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 1t5s:
The structure of Structure of the (Sr)CA2+-Atpase CA2-E1-Amppcp Form also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Structure of the (Sr)CA2+-Atpase CA2-E1-Amppcp Form
(pdb code 1t5s). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Structure of the (Sr)CA2+-Atpase CA2-E1-Amppcp Form, PDB code: 1t5s: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 1t5sGo back to Calcium Binding Sites List in 1t5s
Calcium binding site 1 out
of 2 in the Structure of the (Sr)CA2+-Atpase CA2-E1-Amppcp Form
Mono view Stereo pair view
Calcium binding site 2 out of 2 in 1t5sGo back to Calcium Binding Sites List in 1t5s
Calcium binding site 2 out
of 2 in the Structure of the (Sr)CA2+-Atpase CA2-E1-Amppcp Form
Mono view Stereo pair view
Reference:
T.L.-M.Sorensen,
J.V.Moller,
P.Nissen.
Phosphoryl Transfer and Calcium Ion Occlusion in the Calcium Pump. Science V. 304 1672 2004.
Page generated: Thu Jul 11 22:56:38 2024
ISSN: ISSN 0036-8075 PubMed: 15192230 DOI: 10.1126/SCIENCE.1099366 |
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