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Atomistry » Magnesium » PDB 1t5t-1tkd » 1tbf | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 1t5t-1tkd » 1tbf » |
Magnesium in PDB 1tbf: Catalytic Domain of Human Phosphodiesterase 5A in Complex with SildenafilEnzymatic activity of Catalytic Domain of Human Phosphodiesterase 5A in Complex with Sildenafil
All present enzymatic activity of Catalytic Domain of Human Phosphodiesterase 5A in Complex with Sildenafil:
3.1.4.17; Protein crystallography data
The structure of Catalytic Domain of Human Phosphodiesterase 5A in Complex with Sildenafil, PDB code: 1tbf
was solved by
K.Y.J.Zhang,
G.L.Card,
Y.Suzuki,
D.R.Artis,
D.Fong,
S.Gillette,
D.Hsieh,
J.Neiman,
B.L.West,
C.Zhang,
M.V.Milburn,
S.-H.Kim,
J.Schlessinger,
G.Bollag,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1tbf:
The structure of Catalytic Domain of Human Phosphodiesterase 5A in Complex with Sildenafil also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Catalytic Domain of Human Phosphodiesterase 5A in Complex with Sildenafil
(pdb code 1tbf). 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 5A in Complex with Sildenafil, PDB code: 1tbf: Magnesium binding site 1 out of 1 in 1tbfGo back to![]() ![]()
Magnesium binding site 1 out
of 1 in the Catalytic Domain of Human Phosphodiesterase 5A in Complex with Sildenafil
![]() Mono view ![]() Stereo pair view
Reference:
K.Y.J.Zhang,
G.L.Card,
Y.Suzuki,
D.R.Artis,
D.Fong,
S.Gillette,
D.Hsieh,
J.Neiman,
B.L.West,
C.Zhang,
M.V.Milburn,
S.-H.Kim,
J.Schlessinger,
G.Bollag.
A Glutamine Switch Mechanism For Nucleotide Selectivity By Phosphodiesterases Mol.Cell V. 15 279 2004.
Page generated: Tue Aug 13 14:30:48 2024
ISSN: ISSN 1097-2765 PubMed: 15260978 DOI: 10.1016/J.MOLCEL.2004.07.005 |
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