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Atomistry » Zinc » PDB 1evr-1f62 » 1f0j | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 1evr-1f62 » 1f0j » |
Zinc in PDB 1f0j: Catalytic Domain of Human Phosphodiesterase 4B2BEnzymatic activity of Catalytic Domain of Human Phosphodiesterase 4B2B
All present enzymatic activity of Catalytic Domain of Human Phosphodiesterase 4B2B:
3.1.4.17; Protein crystallography data
The structure of Catalytic Domain of Human Phosphodiesterase 4B2B, PDB code: 1f0j
was solved by
R.X.Xu,
A.M.Hassell,
D.Vanderwall,
M.H.Lambert,
W.D.Holmes,
M.A.Luther,
W.J.Rocque,
M.V.Milburn,
Y.Zhao,
H.Ke,
R.T.Nolte,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1f0j:
The structure of Catalytic Domain of Human Phosphodiesterase 4B2B also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Catalytic Domain of Human Phosphodiesterase 4B2B
(pdb code 1f0j). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Catalytic Domain of Human Phosphodiesterase 4B2B, PDB code: 1f0j: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 1f0jGo back to![]() ![]()
Zinc binding site 1 out
of 2 in the Catalytic Domain of Human Phosphodiesterase 4B2B
![]() Mono view ![]() Stereo pair view
Zinc binding site 2 out of 2 in 1f0jGo back to![]() ![]()
Zinc binding site 2 out
of 2 in the Catalytic Domain of Human Phosphodiesterase 4B2B
![]() Mono view ![]() Stereo pair view
Reference:
R.X.Xu,
A.M.Hassell,
D.Vanderwall,
M.H.Lambert,
W.D.Holmes,
M.A.Luther,
W.J.Rocque,
M.V.Milburn,
Y.Zhao,
H.Ke,
R.T.Nolte.
Atomic Structure of PDE4: Insights Into Phosphodiesterase Mechanism and Specificity. Science V. 288 1822 2000.
Page generated: Sun Oct 13 00:36:03 2024
ISSN: ISSN 0036-8075 PubMed: 10846163 DOI: 10.1126/SCIENCE.288.5472.1822 |
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