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Atomistry » Fluorine » PDB 3hky-3ig6 » 3hvh | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Fluorine » PDB 3hky-3ig6 » 3hvh » |
Fluorine in PDB 3hvh: Rat Catechol O-Methyltransferase in Complex with A Catechol-Type, N6- Methyladenine-Containing Bisubstrate InhibitorEnzymatic activity of Rat Catechol O-Methyltransferase in Complex with A Catechol-Type, N6- Methyladenine-Containing Bisubstrate Inhibitor
All present enzymatic activity of Rat Catechol O-Methyltransferase in Complex with A Catechol-Type, N6- Methyladenine-Containing Bisubstrate Inhibitor:
2.1.1.6; Protein crystallography data
The structure of Rat Catechol O-Methyltransferase in Complex with A Catechol-Type, N6- Methyladenine-Containing Bisubstrate Inhibitor, PDB code: 3hvh
was solved by
A.Ehler,
D.Schlatter,
M.Stihle,
J.Benz,
M.G.Rudolph,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3hvh:
The structure of Rat Catechol O-Methyltransferase in Complex with A Catechol-Type, N6- Methyladenine-Containing Bisubstrate Inhibitor also contains other interesting chemical elements:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Rat Catechol O-Methyltransferase in Complex with A Catechol-Type, N6- Methyladenine-Containing Bisubstrate Inhibitor
(pdb code 3hvh). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Rat Catechol O-Methyltransferase in Complex with A Catechol-Type, N6- Methyladenine-Containing Bisubstrate Inhibitor, PDB code: 3hvh: Fluorine binding site 1 out of 1 in 3hvhGo back to Fluorine Binding Sites List in 3hvh
Fluorine binding site 1 out
of 1 in the Rat Catechol O-Methyltransferase in Complex with A Catechol-Type, N6- Methyladenine-Containing Bisubstrate Inhibitor
Mono view Stereo pair view
Reference:
M.Ellermann,
R.Jakob-Roetne,
C.Lerner,
E.Borroni,
D.Schlatter,
D.Roth,
A.Ehler,
M.G.Rudolph,
F.Diederich.
Molecular Recognition at the Active Site of Catechol-O-Methyltransferase: Energetically Favorable Replacement of A Water Molecule Imported By A Bisubstrate Inhibitor. Angew.Chem.Int.Ed.Engl. V. 48 9092 2009.
Page generated: Wed Jul 31 19:23:50 2024
ISSN: ISSN 1433-7851 PubMed: 19882607 DOI: 10.1002/ANIE.200904410 |
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