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Atomistry » Zinc » PDB 4kxd-4l5v » 4l2l | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 4kxd-4l5v » 4l2l » |
Zinc in PDB 4l2l: Human Leukotriene A4 Hydrolase Complexed with Ligand 4-(4- Benzylphenyl)Thiazol-2-AmineEnzymatic activity of Human Leukotriene A4 Hydrolase Complexed with Ligand 4-(4- Benzylphenyl)Thiazol-2-Amine
All present enzymatic activity of Human Leukotriene A4 Hydrolase Complexed with Ligand 4-(4- Benzylphenyl)Thiazol-2-Amine:
3.3.2.6; Protein crystallography data
The structure of Human Leukotriene A4 Hydrolase Complexed with Ligand 4-(4- Benzylphenyl)Thiazol-2-Amine, PDB code: 4l2l
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 4l2l:
The structure of Human Leukotriene A4 Hydrolase Complexed with Ligand 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 Complexed with Ligand 4-(4- Benzylphenyl)Thiazol-2-Amine
(pdb code 4l2l). 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 Complexed with Ligand 4-(4- Benzylphenyl)Thiazol-2-Amine, PDB code: 4l2l: Zinc binding site 1 out of 1 in 4l2lGo back to Zinc Binding Sites List in 4l2l
Zinc binding site 1 out
of 1 in the Human Leukotriene A4 Hydrolase Complexed with Ligand 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: Wed Dec 16 05:30:31 2020
ISSN: ISSN 0027-8424 PubMed: 24591641 DOI: 10.1073/PNAS.1402136111 |
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