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Atomistry » Fluorine » PDB 3lz3-3n0n » 3m02 » |
Fluorine in PDB 3m02: The Crystal Structure of 5-Epi-Aristolochene Synthase Complexed with (2-Cis,6-Trans)-2-Fluorofarnesyl DiphosphateEnzymatic activity of The Crystal Structure of 5-Epi-Aristolochene Synthase Complexed with (2-Cis,6-Trans)-2-Fluorofarnesyl Diphosphate
All present enzymatic activity of The Crystal Structure of 5-Epi-Aristolochene Synthase Complexed with (2-Cis,6-Trans)-2-Fluorofarnesyl Diphosphate:
4.2.3.9; Protein crystallography data
The structure of The Crystal Structure of 5-Epi-Aristolochene Synthase Complexed with (2-Cis,6-Trans)-2-Fluorofarnesyl Diphosphate, PDB code: 3m02
was solved by
J.P.Noel,
N.Dellas,
J.A.Faraldos,
M.Zhao,
B.A.Hess Jr.,
L.Smentek,
R.M.Coates,
P.E.O'maille,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3m02:
The structure of The Crystal Structure of 5-Epi-Aristolochene Synthase Complexed with (2-Cis,6-Trans)-2-Fluorofarnesyl Diphosphate also contains other interesting chemical elements:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the The Crystal Structure of 5-Epi-Aristolochene Synthase Complexed with (2-Cis,6-Trans)-2-Fluorofarnesyl Diphosphate
(pdb code 3m02). 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 The Crystal Structure of 5-Epi-Aristolochene Synthase Complexed with (2-Cis,6-Trans)-2-Fluorofarnesyl Diphosphate, PDB code: 3m02: Fluorine binding site 1 out of 1 in 3m02Go back to Fluorine Binding Sites List in 3m02
Fluorine binding site 1 out
of 1 in the The Crystal Structure of 5-Epi-Aristolochene Synthase Complexed with (2-Cis,6-Trans)-2-Fluorofarnesyl Diphosphate
Mono view Stereo pair view
Reference:
J.P.Noel,
N.Dellas,
J.A.Faraldos,
M.Zhao,
B.A.Hess,
L.Smentek,
R.M.Coates,
P.E.O'maille.
Structural Elucidation of Cisoid and Transoid Cyclization Pathways of A Sesquiterpene Synthase Using 2-Fluorofarnesyl Diphosphates. Acs Chem.Biol. V. 5 377 2010.
Page generated: Wed Jul 31 20:39:03 2024
ISSN: ISSN 1554-8929 PubMed: 20175559 DOI: 10.1021/CB900295G |
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