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Atomistry » Zinc » PDB 1xm6-1xug » 1xoz | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 1xm6-1xug » 1xoz » |
Zinc in PDB 1xoz: Catalytic Domain of Human Phosphodiesterase 5A in Complex with TadalafilEnzymatic activity of Catalytic Domain of Human Phosphodiesterase 5A in Complex with Tadalafil
All present enzymatic activity of Catalytic Domain of Human Phosphodiesterase 5A in Complex with Tadalafil:
3.1.4.17; Protein crystallography data
The structure of Catalytic Domain of Human Phosphodiesterase 5A in Complex with Tadalafil, PDB code: 1xoz
was solved by
G.L.Card,
B.P.England,
Y.Suzuki,
D.Fong,
B.Powell,
B.Lee,
C.Luu,
M.Tabrizizad,
S.Gillette,
P.N.Ibrahim,
D.R.Artis,
G.Bollag,
M.V.Milburn,
S.-H.Kim,
J.Schlessinger,
K.Y.J.Zhang,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1xoz:
The structure of Catalytic Domain of Human Phosphodiesterase 5A in Complex with Tadalafil also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Catalytic Domain of Human Phosphodiesterase 5A in Complex with Tadalafil
(pdb code 1xoz). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Catalytic Domain of Human Phosphodiesterase 5A in Complex with Tadalafil, PDB code: 1xoz: Zinc binding site 1 out of 1 in 1xozGo back to Zinc Binding Sites List in 1xoz
Zinc binding site 1 out
of 1 in the Catalytic Domain of Human Phosphodiesterase 5A in Complex with Tadalafil
Mono view Stereo pair view
Reference:
G.L.Card,
B.P.England,
Y.Suzuki,
D.Fong,
B.Powell,
B.Lee,
C.Luu,
M.Tabrizizad,
S.Gillette,
P.N.Ibrahim,
D.R.Artis,
G.Bollag,
M.V.Milburn,
S.-H.Kim,
J.Schlessinger,
K.Y.J.Zhang.
Structural Basis For the Activity of Drugs That Inhibit Phosphodiesterases. Structure V. 12 2233 2004.
Page generated: Wed Dec 16 03:13:00 2020
ISSN: ISSN 0969-2126 PubMed: 15576036 DOI: 10.1016/J.STR.2004.10.004 |
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