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Atomistry » Fluorine » PDB 4hxn-4ijh » 4i23 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Fluorine » PDB 4hxn-4ijh » 4i23 » |
Fluorine in PDB 4i23: Crystal Structure of the Wild-Type Egfr Kinase Domain in Complex with Dacomitinib (Soaked)Enzymatic activity of Crystal Structure of the Wild-Type Egfr Kinase Domain in Complex with Dacomitinib (Soaked)
All present enzymatic activity of Crystal Structure of the Wild-Type Egfr Kinase Domain in Complex with Dacomitinib (Soaked):
2.7.10.1; Protein crystallography data
The structure of Crystal Structure of the Wild-Type Egfr Kinase Domain in Complex with Dacomitinib (Soaked), PDB code: 4i23
was solved by
K.S.Gajiwala,
J.Feng,
R.Ferre,
K.Ryan,
O.Brodsky,
A.Stewart,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4i23:
The structure of Crystal Structure of the Wild-Type Egfr Kinase Domain in Complex with Dacomitinib (Soaked) also contains other interesting chemical elements:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Crystal Structure of the Wild-Type Egfr Kinase Domain in Complex with Dacomitinib (Soaked)
(pdb code 4i23). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Crystal Structure of the Wild-Type Egfr Kinase Domain in Complex with Dacomitinib (Soaked), PDB code: 4i23: Fluorine binding site 1 out of 1 in 4i23Go back to![]() ![]()
Fluorine binding site 1 out
of 1 in the Crystal Structure of the Wild-Type Egfr Kinase Domain in Complex with Dacomitinib (Soaked)
![]() Mono view ![]() Stereo pair view
Reference:
K.S.Gajiwala,
J.Feng,
R.Ferre,
K.Ryan,
O.Brodsky,
S.Weinrich,
J.C.Kath,
A.Stewart.
Insights Into the Aberrant Activity of Mutant Egfr Kinase Domain and Drug Recognition. Structure V. 21 209 2013.
Page generated: Mon Jul 14 22:07:47 2025
ISSN: ISSN 0969-2126 PubMed: 23273428 DOI: 10.1016/J.STR.2012.11.014 |
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