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Atomistry » Magnesium » PDB 5f7u-5fjj » 5fhq | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 5f7u-5fjj » 5fhq » |
Magnesium in PDB 5fhq: Crystal Structure of (Wt) Rat Catechol-O-Methyltransferase in Complex with Adomet and 3,5-Dinitrocatechol (Dnc)Enzymatic activity of Crystal Structure of (Wt) Rat Catechol-O-Methyltransferase in Complex with Adomet and 3,5-Dinitrocatechol (Dnc)
All present enzymatic activity of Crystal Structure of (Wt) Rat Catechol-O-Methyltransferase in Complex with Adomet and 3,5-Dinitrocatechol (Dnc):
2.1.1.6; Protein crystallography data
The structure of Crystal Structure of (Wt) Rat Catechol-O-Methyltransferase in Complex with Adomet and 3,5-Dinitrocatechol (Dnc), PDB code: 5fhq
was solved by
C.Levy,
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 Crystal Structure of (Wt) Rat Catechol-O-Methyltransferase in Complex with Adomet and 3,5-Dinitrocatechol (Dnc)
(pdb code 5fhq). 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 Crystal Structure of (Wt) Rat Catechol-O-Methyltransferase in Complex with Adomet and 3,5-Dinitrocatechol (Dnc), PDB code: 5fhq: Magnesium binding site 1 out of 1 in 5fhqGo back to Magnesium Binding Sites List in 5fhq
Magnesium binding site 1 out
of 1 in the Crystal Structure of (Wt) Rat Catechol-O-Methyltransferase in Complex with Adomet and 3,5-Dinitrocatechol (Dnc)
Mono view Stereo pair view
Reference:
B.J.Law,
M.R.Bennett,
M.L.Thompson,
C.Levy,
S.A.Shepherd,
D.Leys,
J.Micklefield.
Effects of Active-Site Modification and Quaternary Structure on the Regioselectivity of Catechol-O-Methyltransferase. Angew.Chem.Int.Ed.Engl. V. 55 2683 2016.
Page generated: Sun Sep 29 04:15:08 2024
ISSN: ESSN 1521-3773 PubMed: 26797714 DOI: 10.1002/ANIE.201508287 |
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