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Fluorine in PDB 3eqb: X-Ray Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (MEK1) in A Complex with Ligand and Mgatp
Enzymatic 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;
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:
| Resolution Low / High (Å) | 20.00 / 2.62 |
| Space group | P 62 |
| Cell size a, b, c (Å), α, β, γ (°) | 82.128, 82.128, 129.099, 90.00, 90.00, 120.00 |
| R / Rfree (%) | 21 / 26.4 |
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 | (Mg) | 1 atom |
| Iodine | (I) | 1 atom |
Fluorine Binding Sites:
The binding sites of Fluorine 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 Fluorine atom.
In total 3 binding sites of Fluorine where 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:
Jump to Fluorine binding site number: 1; 2; 3;
In total 3 binding sites of Fluorine where 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:
Jump to Fluorine binding site number: 1; 2; 3;
Fluorine binding site 1 out of 3 in 3eqb
Go back to
Fluorine Binding Sites List in 3eqb
Fluorine binding site 1 out
of 3 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
Mono view
Stereo pair view
A full contact list of Fluorine with other atoms in the F binding
site number 1 of X-Ray Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (MEK1) in A Complex with Ligand and Mgatp within 5.0Å range:
|
Fluorine binding site 2 out of 3 in 3eqb
Go back to
Fluorine Binding Sites List in 3eqb
Fluorine binding site 2 out
of 3 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
Mono view
Stereo pair view
A full contact list of Fluorine with other atoms in the F binding
site number 2 of X-Ray Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (MEK1) in A Complex with Ligand and Mgatp within 5.0Å range:
|
Fluorine binding site 3 out of 3 in 3eqb
Go back to
Fluorine Binding Sites List in 3eqb
Fluorine binding site 3 out
of 3 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
Mono view
Stereo pair view
A full contact list of Fluorine with other atoms in the F binding
site number 3 of X-Ray Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (MEK1) in A Complex with Ligand and Mgatp within 5.0Å range:
|
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.
ISSN: ISSN 0960-894X
PubMed: 18951019
DOI: 10.1016/J.BMCL.2008.10.015
Page generated: Sun Dec 13 11:45:33 2020
ISSN: ISSN 0960-894X
PubMed: 18951019
DOI: 10.1016/J.BMCL.2008.10.015
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