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Atomistry » Fluorine » PDB 7m04-7mbo » 7m5z » |
Fluorine in PDB 7m5z: Crystal Structure of the Mertk Kinase Domain in Complex with Inhibitor MIPS15692Enzymatic activity of Crystal Structure of the Mertk Kinase Domain in Complex with Inhibitor MIPS15692
All present enzymatic activity of Crystal Structure of the Mertk Kinase Domain in Complex with Inhibitor MIPS15692:
2.7.10.1; Protein crystallography data
The structure of Crystal Structure of the Mertk Kinase Domain in Complex with Inhibitor MIPS15692, PDB code: 7m5z
was solved by
S.J.Hermans,
N.C.Hancock,
J.B.Baell,
M.W.Parker,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Crystal Structure of the Mertk Kinase Domain in Complex with Inhibitor MIPS15692
(pdb code 7m5z). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of the Mertk Kinase Domain in Complex with Inhibitor MIPS15692, PDB code: 7m5z: Jump to Fluorine binding site number: 1; 2; Fluorine binding site 1 out of 2 in 7m5zGo back to Fluorine Binding Sites List in 7m5z
Fluorine binding site 1 out
of 2 in the Crystal Structure of the Mertk Kinase Domain in Complex with Inhibitor MIPS15692
Mono view Stereo pair view
Fluorine binding site 2 out of 2 in 7m5zGo back to Fluorine Binding Sites List in 7m5z
Fluorine binding site 2 out
of 2 in the Crystal Structure of the Mertk Kinase Domain in Complex with Inhibitor MIPS15692
Mono view Stereo pair view
Reference:
S.W.Wong,
L.Vivash,
R.Mudududdla,
N.Nguyen,
S.J.Hermans,
D.M.Shackleford,
J.Field,
L.Xue,
A.Aprico,
N.C.Hancock,
M.Haskali,
M.A.Stashko,
S.V.Frye,
X.Wang,
M.D.Binder,
U.Ackermann,
M.W.Parker,
T.J.Kilpatrick,
J.B.Baell.
Development of [ 18 F]MIPS15692, A Radiotracer with in Vitro Proof-of-Concept For the Imaging of Mer Tyrosine Kinase (Mertk) in Neuroinflammatory Disease. Eur.J.Med.Chem. V. 226 13822 2021.
Page generated: Fri Aug 2 09:23:03 2024
ISSN: ISSN 0223-5234 PubMed: 34563964 DOI: 10.1016/J.EJMECH.2021.113822 |
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