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Atomistry » Chlorine » PDB 7sr6-7t48 » 7t0e | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 7sr6-7t48 » 7t0e » |
Chlorine in PDB 7t0e: Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2BEnzymatic activity of Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2B
All present enzymatic activity of Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2B:
2.5.1.58; Protein crystallography data
The structure of Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2B, PDB code: 7t0e
was solved by
Y.Wang,
Y.Shi,
L.S.Beese,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 7t0e:
The structure of Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2B also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2B
(pdb code 7t0e). 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 Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2B, PDB code: 7t0e: Chlorine binding site 1 out of 1 in 7t0eGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2B
![]() Mono view ![]() Stereo pair view
Reference:
Y.Wang,
F.Xu,
C.B.Nichols,
Y.Shi,
H.W.Hellinga,
J.A.Alspaugh,
M.D.Distefano,
L.S.Beese.
Structure-Guided Discovery of Potent Antifungals That Prevent Ras Signaling By Inhibiting Protein Farnesyltransferase. J.Med.Chem. V. 65 13753 2022.
Page generated: Sun Jul 13 07:16:34 2025
ISSN: ISSN 0022-2623 PubMed: 36218371 DOI: 10.1021/ACS.JMEDCHEM.2C00902 |
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