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Atomistry » Magnesium » PDB 3siy-3srf » 3sn7 » |
Magnesium in PDB 3sn7: Highly Potent, Selective, and Orally Active Phosphodiestarase 10A InhibitorsEnzymatic activity of Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors
All present enzymatic activity of Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors:
3.1.4.17; 3.1.4.35; Protein crystallography data
The structure of Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors, PDB code: 3sn7
was solved by
K.D.Parris,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3sn7:
The structure of Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors
(pdb code 3sn7). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors, PDB code: 3sn7: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 3sn7Go back to![]() ![]()
Magnesium binding site 1 out
of 2 in the Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors
![]() Mono view ![]() Stereo pair view
Magnesium binding site 2 out of 2 in 3sn7Go back to![]() ![]()
Magnesium binding site 2 out
of 2 in the Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors
![]() Mono view ![]() Stereo pair view
Reference:
M.S.Malamas,
Y.Ni,
J.Erdei,
H.Stange,
R.Schindler,
H.J.Lankau,
C.Grunwald,
K.Y.Fan,
K.Parris,
B.Langen,
U.Egerland,
T.Hage,
K.L.Marquis,
S.Grauer,
J.Brennan,
R.Navarra,
R.Graf,
B.L.Harrison,
A.Robichaud,
T.Kronbach,
M.N.Pangalos,
N.Hoefgen,
N.J.Brandon.
Highly Potent, Selective, and Orally Active Phosphodiesterase 10A Inhibitors. J.Med.Chem. V. 54 7621 2011.
Page generated: Thu Aug 15 11:05:46 2024
ISSN: ISSN 0022-2623 PubMed: 21988093 DOI: 10.1021/JM2009138 |
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