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Atomistry » Magnesium » PDB 3o1n-3oha » 3o56 » |
Magnesium in PDB 3o56: Catalytic Domain of Human Phosphodiesterase 4B2B in Complex with A 5- Heterocycle Pyrazolopyridine InhibitorEnzymatic activity of Catalytic Domain of Human Phosphodiesterase 4B2B in Complex with A 5- Heterocycle Pyrazolopyridine Inhibitor
All present enzymatic activity of Catalytic Domain of Human Phosphodiesterase 4B2B in Complex with A 5- Heterocycle Pyrazolopyridine Inhibitor:
3.1.4.17; Protein crystallography data
The structure of Catalytic Domain of Human Phosphodiesterase 4B2B in Complex with A 5- Heterocycle Pyrazolopyridine Inhibitor, PDB code: 3o56
was solved by
D.O.Somers,
M.Neu,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3o56:
The structure of Catalytic Domain of Human Phosphodiesterase 4B2B in Complex with A 5- Heterocycle Pyrazolopyridine Inhibitor also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Catalytic Domain of Human Phosphodiesterase 4B2B in Complex with A 5- Heterocycle Pyrazolopyridine Inhibitor
(pdb code 3o56). 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 Catalytic Domain of Human Phosphodiesterase 4B2B in Complex with A 5- Heterocycle Pyrazolopyridine Inhibitor, PDB code: 3o56: Magnesium binding site 1 out of 1 in 3o56Go back to![]() ![]()
Magnesium binding site 1 out
of 1 in the Catalytic Domain of Human Phosphodiesterase 4B2B in Complex with A 5- Heterocycle Pyrazolopyridine Inhibitor
![]() Mono view ![]() Stereo pair view
Reference:
C.J.Mitchell,
S.P.Ballantine,
D.M.Coe,
C.M.Cook,
C.J.Delves,
M.D.Dowle,
C.D.Edlin,
J.N.Hamblin,
S.Holman,
M.R.Johnson,
P.S.Jones,
S.E.Keeling,
M.Kranz,
M.Lindvall,
F.S.Lucas,
M.Neu,
Y.E.Solanke,
D.O.Somers,
N.A.Trivedi,
J.O.Wiseman.
Pyrazolopyridines As Potent PDE4B Inhibitors: 5-Heterocycle Sar. Bioorg.Med.Chem.Lett. V. 20 5803 2010.
Page generated: Mon Dec 14 08:31:08 2020
ISSN: ISSN 0960-894X PubMed: 20732811 DOI: 10.1016/J.BMCL.2010.07.136 |
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