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Atomistry » Magnesium » PDB 4pjj-4pyj » 4pm0 » |
Magnesium in PDB 4pm0: PDE7A Catalytic Domain in Complex with 2-(Cyclopentylamino)Thieno[3,2- D]Pyrimidin-4(3H)-One DerivativeEnzymatic activity of PDE7A Catalytic Domain in Complex with 2-(Cyclopentylamino)Thieno[3,2- D]Pyrimidin-4(3H)-One Derivative
All present enzymatic activity of PDE7A Catalytic Domain in Complex with 2-(Cyclopentylamino)Thieno[3,2- D]Pyrimidin-4(3H)-One Derivative:
3.1.4.53; Protein crystallography data
The structure of PDE7A Catalytic Domain in Complex with 2-(Cyclopentylamino)Thieno[3,2- D]Pyrimidin-4(3H)-One Derivative, PDB code: 4pm0
was solved by
K.Kawai,
Y.Endo,
T.Asano,
S.Amano,
K.Sawada,
N.Ueo,
N.Takahashi,
Y.Sonoda,
N.Kamei,
N.Nagata,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4pm0:
The structure of PDE7A Catalytic Domain in Complex with 2-(Cyclopentylamino)Thieno[3,2- D]Pyrimidin-4(3H)-One Derivative also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the PDE7A Catalytic Domain in Complex with 2-(Cyclopentylamino)Thieno[3,2- D]Pyrimidin-4(3H)-One Derivative
(pdb code 4pm0). 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 PDE7A Catalytic Domain in Complex with 2-(Cyclopentylamino)Thieno[3,2- D]Pyrimidin-4(3H)-One Derivative, PDB code: 4pm0: Magnesium binding site 1 out of 1 in 4pm0Go back to Magnesium Binding Sites List in 4pm0
Magnesium binding site 1 out
of 1 in the PDE7A Catalytic Domain in Complex with 2-(Cyclopentylamino)Thieno[3,2- D]Pyrimidin-4(3H)-One Derivative
Mono view Stereo pair view
Reference:
K.Kawai,
Y.Endo,
T.Asano,
S.Amano,
K.Sawada,
N.Ueo,
N.Takahashi,
Y.Sonoda,
M.Nagai,
N.Kamei,
N.Nagata.
Discovery of 2-(Cyclopentylamino)Thieno[3,2-D]Pyrimidin-4(3H)-One Derivatives As A New Series of Potent Phosphodiesterase 7 Inhibitors. J.Med.Chem. 2014.
Page generated: Mon Dec 14 19:20:46 2020
ISSN: ISSN 0022-2623 PubMed: 25383422 DOI: 10.1021/JM5008215 |
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