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Atomistry » Chlorine » PDB 3oid-3oow » 3oj8 » |
Chlorine in PDB 3oj8: Alpha-Ketoheterocycle Inhibitors of Fatty Acid Amide Hydrolase Containing Additional Conformational Contraints in the Acyl Side ChainEnzymatic activity of Alpha-Ketoheterocycle Inhibitors of Fatty Acid Amide Hydrolase Containing Additional Conformational Contraints in the Acyl Side Chain
All present enzymatic activity of Alpha-Ketoheterocycle Inhibitors of Fatty Acid Amide Hydrolase Containing Additional Conformational Contraints in the Acyl Side Chain:
3.5.1.99; Protein crystallography data
The structure of Alpha-Ketoheterocycle Inhibitors of Fatty Acid Amide Hydrolase Containing Additional Conformational Contraints in the Acyl Side Chain, PDB code: 3oj8
was solved by
M.Mileni,
R.C.Stevens,
D.L.Boger,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Alpha-Ketoheterocycle Inhibitors of Fatty Acid Amide Hydrolase Containing Additional Conformational Contraints in the Acyl Side Chain
(pdb code 3oj8). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Alpha-Ketoheterocycle Inhibitors of Fatty Acid Amide Hydrolase Containing Additional Conformational Contraints in the Acyl Side Chain, PDB code: 3oj8: Chlorine binding site 1 out of 1 in 3oj8Go back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Alpha-Ketoheterocycle Inhibitors of Fatty Acid Amide Hydrolase Containing Additional Conformational Contraints in the Acyl Side Chain
![]() Mono view ![]() Stereo pair view
Reference:
C.Ezzili,
M.Mileni,
N.Mcglinchey,
J.Z.Long,
S.G.Kinsey,
D.G.Hochstatter,
R.C.Stevens,
A.H.Lichtman,
B.F.Cravatt,
E.J.Bilsky,
D.L.Boger.
Alpha-Ketoheterocycle Inhibitors of Fatty Acid Amide Hydrolase Containing Additional Conformational Contraints in the Acyl Side Chain J.Med.Chem. V. 54 2805 2011.
Page generated: Sun Jul 21 01:42:06 2024
ISSN: ISSN 0022-2623 PubMed: 21428410 DOI: 10.1021/JM101597X |
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