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Atomistry » Fluorine » PDB 6p3u-6pf8 » 6pd8 » |
Fluorine in PDB 6pd8: Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor 39Enzymatic activity of Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor 39
All present enzymatic activity of Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor 39:
2.3.1.48; Protein crystallography data
The structure of Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor 39, PDB code: 6pd8
was solved by
S.J.Hermans,
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 6pd8:
The structure of Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor 39 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 39
(pdb code 6pd8). 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 39, PDB code: 6pd8: Fluorine binding site 1 out of 1 in 6pd8Go back to![]() ![]()
Fluorine binding site 1 out
of 1 in the Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor 39
![]() Mono view ![]() Stereo pair view
Reference:
D.L.Priebbenow,
D.J.Leaver,
N.Nguyen,
B.Cleary,
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,
D.M.Shackleford,
K.Katneni,
M.Cuellar,
J.M.Strasser,
J.L.Dahlin,
M.A.Walters,
I.P.Street,
B.J.Monahan,
K.E.Jarman,
H.Jousset Sabroux,
H.Falk,
M.C.Chung,
S.J.Hermans,
N.L.Downer,
M.W.Parker,
A.K.Voss,
T.Thomas,
J.B.Baell.
Discovery of Acylsulfonohydrazide-Derived Inhibitors of the Lysine Acetyltransferase, KAT6A, As Potent Senescence-Inducing Anti-Cancer Agents. J.Med.Chem. 2020.
Page generated: Fri Aug 2 00:13:13 2024
ISSN: ISSN 0022-2623 PubMed: 32118427 DOI: 10.1021/ACS.JMEDCHEM.9B02071 |
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