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Atomistry » Magnesium » PDB 1qc1-1qs4 » 1qf5 » |
Magnesium in PDB 1qf5: Design, Synthesis, and X-Ray Crystal Structure of An Enzyme Bound Bisubstrate Hybrid Inhibitor of Adenylosuccinate SynthetaseEnzymatic activity of Design, Synthesis, and X-Ray Crystal Structure of An Enzyme Bound Bisubstrate Hybrid Inhibitor of Adenylosuccinate Synthetase
All present enzymatic activity of Design, Synthesis, and X-Ray Crystal Structure of An Enzyme Bound Bisubstrate Hybrid Inhibitor of Adenylosuccinate Synthetase:
6.3.4.4; Protein crystallography data
The structure of Design, Synthesis, and X-Ray Crystal Structure of An Enzyme Bound Bisubstrate Hybrid Inhibitor of Adenylosuccinate Synthetase, PDB code: 1qf5
was solved by
S.Hanessian,
P.-P.Lu,
J.-Y.Sanceau,
P.Chemla,
L.Prade,
K.Gohda,
S.W.Cowan-Jacob,
R.Fonne-Pfister,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Design, Synthesis, and X-Ray Crystal Structure of An Enzyme Bound Bisubstrate Hybrid Inhibitor of Adenylosuccinate Synthetase
(pdb code 1qf5). 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 Design, Synthesis, and X-Ray Crystal Structure of An Enzyme Bound Bisubstrate Hybrid Inhibitor of Adenylosuccinate Synthetase, PDB code: 1qf5: Magnesium binding site 1 out of 1 in 1qf5Go back to![]() ![]()
Magnesium binding site 1 out
of 1 in the Design, Synthesis, and X-Ray Crystal Structure of An Enzyme Bound Bisubstrate Hybrid Inhibitor of Adenylosuccinate Synthetase
![]() Mono view ![]() Stereo pair view
Reference:
S.Hanessian,
P.P.Lu,
J.Y.Sanceau,
P.Chemla,
K.Gohda,
R.Fonne-Pfister,
L.Prade,
S.W.Cowan-Jacob.
An Enzyme-Bound Bisubstrate Hybrid Inhibitor of Adenylosuccinate Synthetase Angew.Chem.Int.Ed.Engl. V. 38 3159 1999.
Page generated: Mon Dec 14 06:38:54 2020
ISSN: ISSN 1433-7851 PubMed: 10556888 DOI: 10.1002/(SICI)1521-3773(19991102)38:21<3159::AID-ANIE3159>3.0.CO;2-2 |
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