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Atomistry » Fluorine » PDB 1w6j-1xz1 » 1xkk | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Fluorine » PDB 1w6j-1xz1 » 1xkk » |
Fluorine in PDB 1xkk: Egfr Kinase Domain Complexed with A Quinazoline Inhibitor- GW572016Enzymatic activity of Egfr Kinase Domain Complexed with A Quinazoline Inhibitor- GW572016
All present enzymatic activity of Egfr Kinase Domain Complexed with A Quinazoline Inhibitor- GW572016:
2.7.1.112; Protein crystallography data
The structure of Egfr Kinase Domain Complexed with A Quinazoline Inhibitor- GW572016, PDB code: 1xkk
was solved by
E.R.Wood,
A.T.Truesdale,
O.B.Mcdonald,
D.Yuan,
A.Hassell,
S.H.Dickerson,
B.Ellis,
C.Pennisi,
E.Horne,
K.Lackey,
K.J.Alligood,
D.W.Rusnak,
T.M.Gilmer,
L.M.Shewchuk,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1xkk:
The structure of Egfr Kinase Domain Complexed with A Quinazoline Inhibitor- GW572016 also contains other interesting chemical elements:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Egfr Kinase Domain Complexed with A Quinazoline Inhibitor- GW572016
(pdb code 1xkk). 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 Egfr Kinase Domain Complexed with A Quinazoline Inhibitor- GW572016, PDB code: 1xkk: Fluorine binding site 1 out of 1 in 1xkkGo back to![]() ![]()
Fluorine binding site 1 out
of 1 in the Egfr Kinase Domain Complexed with A Quinazoline Inhibitor- GW572016
![]() Mono view ![]() Stereo pair view
Reference:
E.R.Wood,
A.T.Truesdale,
O.B.Mcdonald,
D.Yuan,
A.Hassell,
S.H.Dickerson,
B.Ellis,
C.Pennisi,
E.Horne,
K.Lackey,
K.J.Alligood,
D.W.Rusnak,
T.M.Gilmer,
L.Shewchuk.
A Unique Structure For Epidermal Growth Factor Receptor Bound to GW572016 (Lapatinib): Relationships Among Protein Conformation, Inhibitor Off-Rate, and Receptor Activity in Tumor Cells. Cancer Res. V. 64 6652 2004.
Page generated: Mon Jul 14 12:21:08 2025
ISSN: ISSN 0008-5472 PubMed: 15374980 DOI: 10.1158/0008-5472.CAN-04-1168 |
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