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Atomistry » Magnesium » PDB 3ump-3v4f » 3uzs » |
Magnesium in PDB 3uzs: Structure of the C13.28 Rna Aptamer Bound to the G Protein-Coupled Receptor Kinase 2-Heterotrimeric G Protein Beta 1 and Gamma 2 Subunit ComplexEnzymatic activity of Structure of the C13.28 Rna Aptamer Bound to the G Protein-Coupled Receptor Kinase 2-Heterotrimeric G Protein Beta 1 and Gamma 2 Subunit Complex
All present enzymatic activity of Structure of the C13.28 Rna Aptamer Bound to the G Protein-Coupled Receptor Kinase 2-Heterotrimeric G Protein Beta 1 and Gamma 2 Subunit Complex:
2.7.11.15; Protein crystallography data
The structure of Structure of the C13.28 Rna Aptamer Bound to the G Protein-Coupled Receptor Kinase 2-Heterotrimeric G Protein Beta 1 and Gamma 2 Subunit Complex, PDB code: 3uzs
was solved by
J.J.G.Tesmer,
V.M.Tesmer,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Structure of the C13.28 Rna Aptamer Bound to the G Protein-Coupled Receptor Kinase 2-Heterotrimeric G Protein Beta 1 and Gamma 2 Subunit Complex
(pdb code 3uzs). 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 Structure of the C13.28 Rna Aptamer Bound to the G Protein-Coupled Receptor Kinase 2-Heterotrimeric G Protein Beta 1 and Gamma 2 Subunit Complex, PDB code: 3uzs: Magnesium binding site 1 out of 1 in 3uzsGo back to Magnesium Binding Sites List in 3uzs
Magnesium binding site 1 out
of 1 in the Structure of the C13.28 Rna Aptamer Bound to the G Protein-Coupled Receptor Kinase 2-Heterotrimeric G Protein Beta 1 and Gamma 2 Subunit Complex
Mono view Stereo pair view
Reference:
V.M.Tesmer,
S.Lennarz,
G.Mayer,
J.J.Tesmer.
Molecular Mechanism For Inhibition of G Protein-Coupled Receptor Kinase 2 By A Selective Rna Aptamer. Structure V. 20 1300 2012.
Page generated: Thu Aug 15 12:42:02 2024
ISSN: ISSN 0969-2126 PubMed: 22727813 DOI: 10.1016/J.STR.2012.05.002 |
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