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Atomistry » Zinc » PDB 4mhy-4mtd » 4mkt » |
Zinc in PDB 4mkt: Human Leukotriene A4 Hydrolase in Complex with Pro-Gly-Pro Analogue and 4-(4-Benzylphenyl)Thiazol-2-AmineEnzymatic activity of Human Leukotriene A4 Hydrolase in Complex with Pro-Gly-Pro Analogue and 4-(4-Benzylphenyl)Thiazol-2-Amine
All present enzymatic activity of Human Leukotriene A4 Hydrolase in Complex with Pro-Gly-Pro Analogue and 4-(4-Benzylphenyl)Thiazol-2-Amine:
3.3.2.6; Protein crystallography data
The structure of Human Leukotriene A4 Hydrolase in Complex with Pro-Gly-Pro Analogue and 4-(4-Benzylphenyl)Thiazol-2-Amine, PDB code: 4mkt
was solved by
A.Stsiapanava,
A.Rinaldo-Matthis,
J.Z.Haeggstrom,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4mkt:
The structure of Human Leukotriene A4 Hydrolase in Complex with Pro-Gly-Pro Analogue and 4-(4-Benzylphenyl)Thiazol-2-Amine also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Human Leukotriene A4 Hydrolase in Complex with Pro-Gly-Pro Analogue and 4-(4-Benzylphenyl)Thiazol-2-Amine
(pdb code 4mkt). 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 Human Leukotriene A4 Hydrolase in Complex with Pro-Gly-Pro Analogue and 4-(4-Benzylphenyl)Thiazol-2-Amine, PDB code: 4mkt: Zinc binding site 1 out of 1 in 4mktGo back to Zinc Binding Sites List in 4mkt
Zinc binding site 1 out
of 1 in the Human Leukotriene A4 Hydrolase in Complex with Pro-Gly-Pro Analogue and 4-(4-Benzylphenyl)Thiazol-2-Amine
Mono view Stereo pair view
Reference:
A.Stsiapanava,
U.Olsson,
M.Wan,
T.Kleinschmidt,
D.Rutishauser,
R.A.Zubarev,
B.Samuelsson,
A.Rinaldo-Matthis,
J.Z.Haeggstrom.
Binding of Pro-Gly-Pro at the Active Site of Leukotriene A4 Hydrolase/Aminopeptidase and Development of An Epoxide Hydrolase Selective Inhibitor. Proc.Natl.Acad.Sci.Usa V. 111 4227 2014.
Page generated: Sun Oct 27 02:32:47 2024
ISSN: ISSN 0027-8424 PubMed: 24591641 DOI: 10.1073/PNAS.1402136111 |
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