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Atomistry » Bromine » PDB 7r3i-7v45 » 7t0e | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Bromine » PDB 7r3i-7v45 » 7t0e » |
Bromine 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:
Bromine Binding Sites:
The binding sites of Bromine 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 Bromine atom.
In total only one binding site of Bromine was determined in the Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2B, PDB code: 7t0e: Bromine binding site 1 out of 1 in 7t0eGo back to Bromine Binding Sites List in 7t0e
Bromine 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: Thu Jul 11 04:35:18 2024
ISSN: ISSN 0022-2623 PubMed: 36218371 DOI: 10.1021/ACS.JMEDCHEM.2C00902 |
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