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Atomistry » Ytterbium » PDB 3ftz-5i2s » 3ftz » |
Ytterbium in PDB 3ftz: Leukotriene A4 Hydrolase in Complex with Fragment 2-(Pyridin-3- Ylmethoxy)AnilineEnzymatic activity of Leukotriene A4 Hydrolase in Complex with Fragment 2-(Pyridin-3- Ylmethoxy)Aniline
All present enzymatic activity of Leukotriene A4 Hydrolase in Complex with Fragment 2-(Pyridin-3- Ylmethoxy)Aniline:
3.3.2.6; Protein crystallography data
The structure of Leukotriene A4 Hydrolase in Complex with Fragment 2-(Pyridin-3- Ylmethoxy)Aniline, PDB code: 3ftz
was solved by
D.R.Davies,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3ftz:
The structure of Leukotriene A4 Hydrolase in Complex with Fragment 2-(Pyridin-3- Ylmethoxy)Aniline also contains other interesting chemical elements:
Ytterbium Binding Sites:
The binding sites of Ytterbium atom in the Leukotriene A4 Hydrolase in Complex with Fragment 2-(Pyridin-3- Ylmethoxy)Aniline
(pdb code 3ftz). This binding sites where shown within
5.0 Angstroms radius around Ytterbium atom.
In total only one binding site of Ytterbium was determined in the Leukotriene A4 Hydrolase in Complex with Fragment 2-(Pyridin-3- Ylmethoxy)Aniline, PDB code: 3ftz: Ytterbium binding site 1 out of 1 in 3ftzGo back to![]() ![]()
Ytterbium binding site 1 out
of 1 in the Leukotriene A4 Hydrolase in Complex with Fragment 2-(Pyridin-3- Ylmethoxy)Aniline
![]() Mono view ![]() Stereo pair view
Reference:
V.Sandanayaka,
B.Mamat,
R.K.Mishra,
J.Winger,
M.Krohn,
L.M.Zhou,
M.Keyvan,
L.Enache,
D.Sullins,
E.Onua,
J.Zhang,
G.Halldorsdottir,
H.Sigthorsdottir,
A.Thorlaksdottir,
G.Sigthorsson,
M.Thorsteinnsdottir,
D.R.Davies,
L.J.Stewart,
D.E.Zembower,
T.Andresson,
A.S.Kiselyov,
J.Singh,
M.E.Gurney.
Discovery of 4-[(2S)-2-{[4-(4-Chlorophenoxy)Phenoxy]Methyl}-1- Pyrrolidinyl]Butanoic Acid (Dg-051) As A Novel Leukotriene A4 Hydrolase Inhibitor of Leukotriene B4 Biosynthesis. J.Med.Chem. V. 53 573 2010.
Page generated: Sat Oct 12 21:07:06 2024
ISSN: ISSN 0022-2623 PubMed: 19950900 DOI: 10.1021/JM900838G |
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