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Fluorine in PDB 1jdj: Crystal Structure of Leishmania Mexicana Glycerol-3-Phosphate Dehydrogenase in Complex with 2-Fluoro-6-ChloropurineEnzymatic activity of Crystal Structure of Leishmania Mexicana Glycerol-3-Phosphate Dehydrogenase in Complex with 2-Fluoro-6-Chloropurine
All present enzymatic activity of Crystal Structure of Leishmania Mexicana Glycerol-3-Phosphate Dehydrogenase in Complex with 2-Fluoro-6-Chloropurine:
1.1.1.8; Protein crystallography data
The structure of Crystal Structure of Leishmania Mexicana Glycerol-3-Phosphate Dehydrogenase in Complex with 2-Fluoro-6-Chloropurine, PDB code: 1jdj
was solved by
S.Suresh,
G.Wisedchaisri,
K.J.Kennedy,
C.L.M.J.Verlinde,
M.H.Gelb,
W.G.J.Hol,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1jdj:
The structure of Crystal Structure of Leishmania Mexicana Glycerol-3-Phosphate Dehydrogenase in Complex with 2-Fluoro-6-Chloropurine also contains other interesting chemical elements:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Crystal Structure of Leishmania Mexicana Glycerol-3-Phosphate Dehydrogenase in Complex with 2-Fluoro-6-Chloropurine
(pdb code 1jdj). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Crystal Structure of Leishmania Mexicana Glycerol-3-Phosphate Dehydrogenase in Complex with 2-Fluoro-6-Chloropurine, PDB code: 1jdj: Fluorine binding site 1 out of 1 in 1jdjGo back to Fluorine Binding Sites List in 1jdj
Fluorine binding site 1 out
of 1 in the Crystal Structure of Leishmania Mexicana Glycerol-3-Phosphate Dehydrogenase in Complex with 2-Fluoro-6-Chloropurine
Mono view Stereo pair view
Reference:
J.Choe,
S.Suresh,
G.Wisedchaisri,
K.J.Kennedy,
M.H.Gelb,
W.G.Hol.
Anomalous Differences of Light Elements in Determining Precise Binding Modes of Ligands to Glycerol-3-Phosphate Dehydrogenase. Chem.Biol. V. 9 1189 2002.
Page generated: Sun Dec 13 11:30:29 2020
ISSN: ISSN 1074-5521 PubMed: 12445769 DOI: 10.1016/S1074-5521(02)00243-0 |
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