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Atomistry » Zinc » PDB 5aeh-5ami » 5aen » |
Zinc in PDB 5aen: Structure of Human Leukotriene A4 Hydrolase in Complex with Inhibitor Dimethyl(2-(4-Phenoxyphenoxy)Ethyl)AmineEnzymatic activity of Structure of Human Leukotriene A4 Hydrolase in Complex with Inhibitor Dimethyl(2-(4-Phenoxyphenoxy)Ethyl)Amine
All present enzymatic activity of Structure of Human Leukotriene A4 Hydrolase in Complex with Inhibitor Dimethyl(2-(4-Phenoxyphenoxy)Ethyl)Amine:
3.3.2.6; Protein crystallography data
The structure of Structure of Human Leukotriene A4 Hydrolase in Complex with Inhibitor Dimethyl(2-(4-Phenoxyphenoxy)Ethyl)Amine, PDB code: 5aen
was solved by
D.Moser,
S.K.Wittmann,
J.Kramer,
R.Blocher,
J.Achenbach,
D.Pogoryelov,
E.Proschak,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5aen:
The structure of Structure of Human Leukotriene A4 Hydrolase in Complex with Inhibitor Dimethyl(2-(4-Phenoxyphenoxy)Ethyl)Amine also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Structure of Human Leukotriene A4 Hydrolase in Complex with Inhibitor Dimethyl(2-(4-Phenoxyphenoxy)Ethyl)Amine
(pdb code 5aen). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Structure of Human Leukotriene A4 Hydrolase in Complex with Inhibitor Dimethyl(2-(4-Phenoxyphenoxy)Ethyl)Amine, PDB code: 5aen: Zinc binding site 1 out of 1 in 5aenGo back to Zinc Binding Sites List in 5aen
Zinc binding site 1 out
of 1 in the Structure of Human Leukotriene A4 Hydrolase in Complex with Inhibitor Dimethyl(2-(4-Phenoxyphenoxy)Ethyl)Amine
Mono view Stereo pair view
Reference:
D.Moser,
S.K.Wittmann,
J.Kramer,
R.Blocher,
J.Achenbach,
D.Pogoryelov,
E.Proschak.
Peng: A Neural Gas-Based Approach For Pharmacophore Elucidation. Method Design, Validation and Virtual Screening For Novel Ligands of LTA4H. J.Chem.Inf.Model. 2015.
Page generated: Sun Oct 27 12:58:22 2024
ISSN: ESSN 1549-960X PubMed: 25625859 DOI: 10.1021/CI500618U |
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