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Atomistry » Fluorine » PDB 6oaq-6onv » 6oip » |
Fluorine in PDB 6oip: Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor 34Enzymatic activity of Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor 34
All present enzymatic activity of Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor 34:
2.3.1.48; Protein crystallography data
The structure of Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor 34, PDB code: 6oip
was solved by
S.J.Hermans,
M.C.Chung,
M.W.Parker,
T.Thomas,
J.B.Baell,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6oip:
The structure of Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor 34 also contains other interesting chemical elements:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor 34
(pdb code 6oip). 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 Myst Acetyltransferase Domain in Complex with Inhibitor 34, PDB code: 6oip: Fluorine binding site 1 out of 1 in 6oipGo back to![]() ![]()
Fluorine binding site 1 out
of 1 in the Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor 34
![]() Mono view ![]() Stereo pair view
Reference:
D.J.Leaver,
B.Cleary,
N.Nguyen,
D.L.Priebbenow,
H.R.Lagiakos,
J.Sanchez,
L.Xue,
F.Huang,
Y.Sun,
P.Mujumdar,
R.Mudududdla,
S.Varghese,
S.Teguh,
S.A.Charman,
K.L.White,
K.Katneni,
M.Cuellar,
J.M.Strasser,
J.L.Dahlin,
M.A.Walters,
I.P.Street,
B.J.Monahan,
K.E.Jarman,
H.J.Sabroux,
H.Falk,
M.C.Chung,
S.J.Hermans,
M.W.Parker,
T.Thomas,
J.B.Baell.
Discovery of Benzoylsulfonohydrazides As Potent Inhibitors of the Histone Acetyltransferase KAT6A. J.Med.Chem. V. 62 7146 2019.
Page generated: Tue Jul 15 14:14:06 2025
ISSN: ISSN 0022-2623 PubMed: 31256587 DOI: 10.1021/ACS.JMEDCHEM.9B00665 |
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