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Atomistry » Magnesium » PDB 3jay-3jwr » 3jb9 » |
Magnesium in PDB 3jb9: Cryo-Em Structure of the Yeast Spliceosome at 3.6 Angstrom ResolutionEnzymatic activity of Cryo-Em Structure of the Yeast Spliceosome at 3.6 Angstrom Resolution
All present enzymatic activity of Cryo-Em Structure of the Yeast Spliceosome at 3.6 Angstrom Resolution:
5.2.1.8; Other elements in 3jb9:
The structure of Cryo-Em Structure of the Yeast Spliceosome at 3.6 Angstrom Resolution also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Cryo-Em Structure of the Yeast Spliceosome at 3.6 Angstrom Resolution
(pdb code 3jb9). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Cryo-Em Structure of the Yeast Spliceosome at 3.6 Angstrom Resolution, PDB code: 3jb9: Jump to Magnesium binding site number: 1; 2; 3; 4; Magnesium binding site 1 out of 4 in 3jb9Go back to Magnesium Binding Sites List in 3jb9
Magnesium binding site 1 out
of 4 in the Cryo-Em Structure of the Yeast Spliceosome at 3.6 Angstrom Resolution
Mono view Stereo pair view
Magnesium binding site 2 out of 4 in 3jb9Go back to Magnesium Binding Sites List in 3jb9
Magnesium binding site 2 out
of 4 in the Cryo-Em Structure of the Yeast Spliceosome at 3.6 Angstrom Resolution
Mono view Stereo pair view
Magnesium binding site 3 out of 4 in 3jb9Go back to Magnesium Binding Sites List in 3jb9
Magnesium binding site 3 out
of 4 in the Cryo-Em Structure of the Yeast Spliceosome at 3.6 Angstrom Resolution
Mono view Stereo pair view
Magnesium binding site 4 out of 4 in 3jb9Go back to Magnesium Binding Sites List in 3jb9
Magnesium binding site 4 out
of 4 in the Cryo-Em Structure of the Yeast Spliceosome at 3.6 Angstrom Resolution
Mono view Stereo pair view
Reference:
C.Yan,
J.Hang,
R.Wan,
M.Huang,
C.Wong,
Y.Shi.
Structure of A Yeast Spliceosome at 3.6-Angstrom Resolution Science V. 349 1182 2015.
Page generated: Wed Aug 14 17:08:30 2024
ISSN: ISSN 0036-8075 PubMed: 26292707 DOI: 10.1126/SCIENCE.AAC7629 |
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