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Atomistry » Zinc » PDB 3c3u-3cia » 3cho » |
Zinc in PDB 3cho: Crystal Structure of Leukotriene A4 Hydrolase in Complex with 2-Amino- N-[4-(Phenylmethoxy)Phenyl]-AcetamideEnzymatic activity of Crystal Structure of Leukotriene A4 Hydrolase in Complex with 2-Amino- N-[4-(Phenylmethoxy)Phenyl]-Acetamide
All present enzymatic activity of Crystal Structure of Leukotriene A4 Hydrolase in Complex with 2-Amino- N-[4-(Phenylmethoxy)Phenyl]-Acetamide:
3.3.2.6; Protein crystallography data
The structure of Crystal Structure of Leukotriene A4 Hydrolase in Complex with 2-Amino- N-[4-(Phenylmethoxy)Phenyl]-Acetamide, PDB code: 3cho
was solved by
M.M.G.M.Thunnissen,
M.Adler,
M.Whitlow,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3cho:
The structure of Crystal Structure of Leukotriene A4 Hydrolase in Complex with 2-Amino- N-[4-(Phenylmethoxy)Phenyl]-Acetamide also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Leukotriene A4 Hydrolase in Complex with 2-Amino- N-[4-(Phenylmethoxy)Phenyl]-Acetamide
(pdb code 3cho). 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 Crystal Structure of Leukotriene A4 Hydrolase in Complex with 2-Amino- N-[4-(Phenylmethoxy)Phenyl]-Acetamide, PDB code: 3cho: Zinc binding site 1 out of 1 in 3choGo back to![]() ![]()
Zinc binding site 1 out
of 1 in the Crystal Structure of Leukotriene A4 Hydrolase in Complex with 2-Amino- N-[4-(Phenylmethoxy)Phenyl]-Acetamide
![]() Mono view ![]() Stereo pair view
Reference:
T.A.Kirkland,
M.Adler,
J.G.Bauman,
M.Chen,
J.Z.Haeggstrom,
B.King,
M.J.Kochanny,
A.M.Liang,
L.Mendoza,
G.B.Phillips,
M.Thunnissen,
L.Trinh,
M.Whitlow,
B.Ye,
H.Ye,
J.Parkinson,
W.J.Guilford.
Synthesis of Glutamic Acid Analogs As Potent Inhibitors of Leukotriene A4 Hydrolase. Bioorg.Med.Chem. V. 16 4963 2008.
Page generated: Wed Dec 16 04:10:38 2020
ISSN: ISSN 0968-0896 PubMed: 18394906 DOI: 10.1016/J.BMC.2008.03.042 |
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