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Atomistry » Iodine » PDB 3kxf-3onn » 3mbl » |
Iodine in PDB 3mbl: Crystal Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (Mek 1) in Complex with Ligand and MgadpEnzymatic activity of Crystal Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (Mek 1) in Complex with Ligand and Mgadp
All present enzymatic activity of Crystal Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (Mek 1) in Complex with Ligand and Mgadp:
2.7.12.2; Protein crystallography data
The structure of Crystal Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (Mek 1) in Complex with Ligand and Mgadp, PDB code: 3mbl
was solved by
D.R.Dougan,
C.D.Mol,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3mbl:
The structure of Crystal Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (Mek 1) in Complex with Ligand and Mgadp also contains other interesting chemical elements:
Iodine Binding Sites:
The binding sites of Iodine atom in the Crystal Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (Mek 1) in Complex with Ligand and Mgadp
(pdb code 3mbl). This binding sites where shown within
5.0 Angstroms radius around Iodine atom.
In total only one binding site of Iodine was determined in the Crystal Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (Mek 1) in Complex with Ligand and Mgadp, PDB code: 3mbl: Iodine binding site 1 out of 1 in 3mblGo back to![]() ![]()
Iodine binding site 1 out
of 1 in the Crystal Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (Mek 1) in Complex with Ligand and Mgadp
![]() Mono view ![]() Stereo pair view
Reference:
M.B.Wallace,
M.E.Adams,
T.Kanouni,
C.D.Mol,
D.R.Dougan,
V.A.Feher,
S.M.O'connell,
L.Shi,
P.Halkowycz,
Q.Dong.
Structure-Based Design and Synthesis of Pyrrole Derivatives As Mek Inhibitors. Bioorg.Med.Chem.Lett. V. 20 4156 2010.
Page generated: Sun Dec 13 19:28:21 2020
ISSN: ISSN 0960-894X PubMed: 20621728 DOI: 10.1016/J.BMCL.2010.05.058 |
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