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Atomistry » Magnesium » PDB 3efq-3eql » 3eqb » |
Magnesium in PDB 3eqb: X-Ray Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (MEK1) in A Complex with Ligand and MgatpEnzymatic activity of X-Ray Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (MEK1) in A Complex with Ligand and Mgatp
All present enzymatic activity of X-Ray Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (MEK1) in A Complex with Ligand and Mgatp:
2.7.12.2; Protein crystallography data
The structure of X-Ray Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (MEK1) in A Complex with Ligand and Mgatp, PDB code: 3eqb
was solved by
J.F.Ohren,
A.Pavlovsky,
E.Zhang,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3eqb:
The structure of X-Ray Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (MEK1) in A Complex with Ligand and Mgatp also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the X-Ray Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (MEK1) in A Complex with Ligand and Mgatp
(pdb code 3eqb). 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 X-Ray Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (MEK1) in A Complex with Ligand and Mgatp, PDB code: 3eqb: Magnesium binding site 1 out of 1 in 3eqbGo back to Magnesium Binding Sites List in 3eqb
Magnesium binding site 1 out
of 1 in the X-Ray Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (MEK1) in A Complex with Ligand and Mgatp
Mono view Stereo pair view
Reference:
J.S.Warmus,
C.Flamme,
L.Y.Zhang,
S.Barrett,
A.Bridges,
H.Chen,
R.Gowan,
M.Kaufman,
J.Sebolt-Leopold,
W.Leopold,
R.Merriman,
J.Ohren,
A.Pavlovsky,
S.Przybranowski,
H.Tecle,
H.Valik,
C.Whitehead,
E.Zhang.
2-Alkylamino- and Alkoxy-Substituted 2-Amino-1,3,4-Oxadiazoles-O-Alkyl Benzohydroxamate Esters Replacements Retain the Desired Inhibition and Selectivity Against Mek (Map Erk Kinase). Bioorg.Med.Chem.Lett. V. 18 6171 2008.
Page generated: Mon Dec 14 08:06:47 2020
ISSN: ISSN 0960-894X PubMed: 18951019 DOI: 10.1016/J.BMCL.2008.10.015 |
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