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Atomistry » Magnesium » PDB 1qc5-1qsh » 1qf4 » |
Magnesium in PDB 1qf4: 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: 1qf4
was solved by
S.Hanessian,
P.-P.Lu,
J.-Y.Sanceau,
P.Chemla,
K.Gohda,
R.Fonne-Pfister,
L.Prade,
S.W.Cowan-Jacob,
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 1qf4). 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: 1qf4: Magnesium binding site 1 out of 1 in 1qf4Go 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: Tue Aug 13 11:49:34 2024
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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