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Atomistry » Chlorine » PDB 4e0j-4e9v » 4e93 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 4e0j-4e9v » 4e93 » |
Chlorine in PDB 4e93: Crystal Structure of Human Feline Sarcoma Viral Oncogene Homologue (V- Fes)in Complex with TAE684Enzymatic activity of Crystal Structure of Human Feline Sarcoma Viral Oncogene Homologue (V- Fes)in Complex with TAE684
All present enzymatic activity of Crystal Structure of Human Feline Sarcoma Viral Oncogene Homologue (V- Fes)in Complex with TAE684:
2.7.10.2; Protein crystallography data
The structure of Crystal Structure of Human Feline Sarcoma Viral Oncogene Homologue (V- Fes)in Complex with TAE684, PDB code: 4e93
was solved by
P.Filippakopoulos,
E.Salah,
C.V.Miduturu,
O.Fedorov,
C.Cooper,
F.Vondelft,
C.H.Arrowsmith,
A.M.Edwards,
J.Weigelt,
N.S.Gray,
S.Knapp,
Structural Genomics Consortium (Sgc),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Human Feline Sarcoma Viral Oncogene Homologue (V- Fes)in Complex with TAE684
(pdb code 4e93). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Human Feline Sarcoma Viral Oncogene Homologue (V- Fes)in Complex with TAE684, PDB code: 4e93: Chlorine binding site 1 out of 1 in 4e93Go back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Crystal Structure of Human Feline Sarcoma Viral Oncogene Homologue (V- Fes)in Complex with TAE684
![]() Mono view ![]() Stereo pair view
Reference:
S.Hellwig,
C.V.Miduturu,
S.Kanda,
J.Zhang,
P.Filippakopoulos,
E.Salah,
X.Deng,
H.G.Choi,
W.Zhou,
W.Hur,
S.Knapp,
N.S.Gray,
T.E.Smithgall.
Small-Molecule Inhibitors of the C-Fes Protein-Tyrosine Kinase. Chem.Biol. V. 19 529 2012.
Page generated: Fri Jul 11 14:42:32 2025
ISSN: ISSN 1074-5521 PubMed: 22520759 DOI: 10.1016/J.CHEMBIOL.2012.01.020 |
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