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Atomistry » Fluorine » PDB 5j8m-5jw1 » 5jv1 » |
Fluorine in PDB 5jv1: Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Cl-08-066Enzymatic activity of Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Cl-08-066
All present enzymatic activity of Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Cl-08-066:
2.5.1.1; 2.5.1.10; Protein crystallography data
The structure of Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Cl-08-066, PDB code: 5jv1
was solved by
J.Park,
C.Y.Leung,
Y.S.Tsantrizos,
A.M.Berghuis,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5jv1:
The structure of Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Cl-08-066 also contains other interesting chemical elements:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Cl-08-066
(pdb code 5jv1). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Cl-08-066, PDB code: 5jv1: Jump to Fluorine binding site number: 1; 2; Fluorine binding site 1 out of 2 in 5jv1Go back to Fluorine Binding Sites List in 5jv1
Fluorine binding site 1 out
of 2 in the Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Cl-08-066
Mono view Stereo pair view
Fluorine binding site 2 out of 2 in 5jv1Go back to Fluorine Binding Sites List in 5jv1
Fluorine binding site 2 out
of 2 in the Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Cl-08-066
Mono view Stereo pair view
Reference:
J.Park,
C.Y.Leung,
A.N.Matralis,
C.M.Lacbay,
M.Tsakos,
G.Fernandez De Troconiz,
A.M.Berghuis,
Y.S.Tsantrizos.
Pharmacophore Mapping of Thienopyrimidine-Based Monophosphonate (Thp-Mp) Inhibitors of the Human Farnesyl Pyrophosphate Synthase. J. Med. Chem. V. 60 2119 2017.
Page generated: Thu Aug 1 10:42:57 2024
ISSN: ISSN 1520-4804 PubMed: 28208018 DOI: 10.1021/ACS.JMEDCHEM.6B01888 |
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