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Atomistry » Calcium » PDB 2rf7-2tep » 2sns » |
Calcium in PDB 2sns: Staphylococcal Nuclease. Proposed Mechanism of Action Based on Structure of Enzyme-Thymidine 3(Prime),5(Prime)-Biphosphate-Calcium Ion Complex at 1.5-Angstroms ResolutionEnzymatic activity of Staphylococcal Nuclease. Proposed Mechanism of Action Based on Structure of Enzyme-Thymidine 3(Prime),5(Prime)-Biphosphate-Calcium Ion Complex at 1.5-Angstroms Resolution
All present enzymatic activity of Staphylococcal Nuclease. Proposed Mechanism of Action Based on Structure of Enzyme-Thymidine 3(Prime),5(Prime)-Biphosphate-Calcium Ion Complex at 1.5-Angstroms Resolution:
3.1.31.1; Protein crystallography data
The structure of Staphylococcal Nuclease. Proposed Mechanism of Action Based on Structure of Enzyme-Thymidine 3(Prime),5(Prime)-Biphosphate-Calcium Ion Complex at 1.5-Angstroms Resolution, PDB code: 2sns
was solved by
M.J.Legg,
F.A.Cotton,
E.E.Hazen Jr.,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Calcium Binding Sites:
The binding sites of Calcium atom in the Staphylococcal Nuclease. Proposed Mechanism of Action Based on Structure of Enzyme-Thymidine 3(Prime),5(Prime)-Biphosphate-Calcium Ion Complex at 1.5-Angstroms Resolution
(pdb code 2sns). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Staphylococcal Nuclease. Proposed Mechanism of Action Based on Structure of Enzyme-Thymidine 3(Prime),5(Prime)-Biphosphate-Calcium Ion Complex at 1.5-Angstroms Resolution, PDB code: 2sns: Calcium binding site 1 out of 1 in 2snsGo back to Calcium Binding Sites List in 2sns
Calcium binding site 1 out
of 1 in the Staphylococcal Nuclease. Proposed Mechanism of Action Based on Structure of Enzyme-Thymidine 3(Prime),5(Prime)-Biphosphate-Calcium Ion Complex at 1.5-Angstroms Resolution
Mono view Stereo pair view
Reference:
F.A.Cotton,
E.E.Hazen Jr.,
M.J.Legg.
Thesis, Texas Agricultural 1977AND Mechanical University.
Page generated: Sat Dec 12 03:52:33 2020
ISSN: ISSN 0531-5131 |
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