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Atomistry » Calcium » PDB 3s9w-3snz » 3sd6 » |
Calcium in PDB 3sd6: Crystal Structure of the Amino-Terminal Domain of Human Cardiac Troponin C in Complex with Cadmium at 1.4 Resolution.Protein crystallography data
The structure of Crystal Structure of the Amino-Terminal Domain of Human Cardiac Troponin C in Complex with Cadmium at 1.4 Resolution., PDB code: 3sd6
was solved by
X.L.Zhang,
M.Paetzel,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3sd6:
The structure of Crystal Structure of the Amino-Terminal Domain of Human Cardiac Troponin C in Complex with Cadmium at 1.4 Resolution. also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Crystal Structure of the Amino-Terminal Domain of Human Cardiac Troponin C in Complex with Cadmium at 1.4 Resolution.
(pdb code 3sd6). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of the Amino-Terminal Domain of Human Cardiac Troponin C in Complex with Cadmium at 1.4 Resolution., PDB code: 3sd6: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 3sd6Go back to Calcium Binding Sites List in 3sd6
Calcium binding site 1 out
of 2 in the Crystal Structure of the Amino-Terminal Domain of Human Cardiac Troponin C in Complex with Cadmium at 1.4 Resolution.
Mono view Stereo pair view
Calcium binding site 2 out of 2 in 3sd6Go back to Calcium Binding Sites List in 3sd6
Calcium binding site 2 out
of 2 in the Crystal Structure of the Amino-Terminal Domain of Human Cardiac Troponin C in Complex with Cadmium at 1.4 Resolution.
Mono view Stereo pair view
Reference:
X.L.Zhang,
G.F.Tibbits,
M.Paetzel.
The Structure of Cardiac Troponin C Regulatory Domain with Bound Cd(2+) Reveals A Closed Conformation and Unique Ion Coordination. Acta Crystallogr.,Sect.D V. 69 722 2013.
Page generated: Sat Jul 13 19:09:52 2024
ISSN: ISSN 0907-4449 PubMed: 23633581 DOI: 10.1107/S0907444913001182 |
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