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Atomistry » Magnesium » PDB 4kvw-4l9z » 4l87 » |
Magnesium in PDB 4l87: Crystal Structure of the Human Seryl-Trna Synthetase in Complex with Ser-Sa at 2.9 Angstrom ResolutionEnzymatic activity of Crystal Structure of the Human Seryl-Trna Synthetase in Complex with Ser-Sa at 2.9 Angstrom Resolution
All present enzymatic activity of Crystal Structure of the Human Seryl-Trna Synthetase in Complex with Ser-Sa at 2.9 Angstrom Resolution:
6.1.1.11; Protein crystallography data
The structure of Crystal Structure of the Human Seryl-Trna Synthetase in Complex with Ser-Sa at 2.9 Angstrom Resolution, PDB code: 4l87
was solved by
X.Xu,
X.-L.Yang,
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 Crystal Structure of the Human Seryl-Trna Synthetase in Complex with Ser-Sa at 2.9 Angstrom Resolution
(pdb code 4l87). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the Human Seryl-Trna Synthetase in Complex with Ser-Sa at 2.9 Angstrom Resolution, PDB code: 4l87: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 4l87Go back to Magnesium Binding Sites List in 4l87
Magnesium binding site 1 out
of 2 in the Crystal Structure of the Human Seryl-Trna Synthetase in Complex with Ser-Sa at 2.9 Angstrom Resolution
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 4l87Go back to Magnesium Binding Sites List in 4l87
Magnesium binding site 2 out
of 2 in the Crystal Structure of the Human Seryl-Trna Synthetase in Complex with Ser-Sa at 2.9 Angstrom Resolution
Mono view Stereo pair view
Reference:
X.Xu,
Y.Shi,
X.L.Yang.
Crystal Structure of Human Seryl-Trna Synthetase and Ser-Sa Complex Reveals A Molecular Lever Specific to Higher Eukaryotes. Structure V. 21 2078 2013.
Page generated: Sat Aug 17 04:28:45 2024
ISSN: ISSN 0969-2126 PubMed: 24095058 DOI: 10.1016/J.STR.2013.08.021 |
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