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Atomistry » Zinc » PDB 1sxa-1tbf » 1tb5 » |
Zinc in PDB 1tb5: Catalytic Domain of Human Phosphodiesterase 4B in Complex with AmpEnzymatic activity of Catalytic Domain of Human Phosphodiesterase 4B in Complex with Amp
All present enzymatic activity of Catalytic Domain of Human Phosphodiesterase 4B in Complex with Amp:
3.1.4.17; Protein crystallography data
The structure of Catalytic Domain of Human Phosphodiesterase 4B in Complex with Amp, PDB code: 1tb5
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 1tb5:
The structure of Catalytic Domain of Human Phosphodiesterase 4B in Complex with Amp also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Catalytic Domain of Human Phosphodiesterase 4B in Complex with Amp
(pdb code 1tb5). 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 4B in Complex with Amp, PDB code: 1tb5: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 1tb5Go back to Zinc Binding Sites List in 1tb5
Zinc binding site 1 out
of 2 in the Catalytic Domain of Human Phosphodiesterase 4B in Complex with Amp
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 1tb5Go back to Zinc Binding Sites List in 1tb5
Zinc binding site 2 out
of 2 in the Catalytic Domain of Human Phosphodiesterase 4B in Complex with Amp
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: Wed Oct 16 19:04:49 2024
ISSN: ISSN 1097-2765 PubMed: 15260978 DOI: 10.1016/J.MOLCEL.2004.07.005 |
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