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Atomistry » Fluorine » PDB 6oac-6onm » 6oiq » |
Fluorine in PDB 6oiq: Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor 63Enzymatic activity of Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor 63
All present enzymatic activity of Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor 63:
2.3.1.48; Protein crystallography data
The structure of Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor 63, PDB code: 6oiq
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 6oiq:
The structure of Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor 63 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 63
(pdb code 6oiq). 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 63, PDB code: 6oiq: Fluorine binding site 1 out of 1 in 6oiqGo back to Fluorine Binding Sites List in 6oiq
Fluorine binding site 1 out
of 1 in the Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor 63
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: Thu Aug 1 23:41:59 2024
ISSN: ISSN 0022-2623 PubMed: 31256587 DOI: 10.1021/ACS.JMEDCHEM.9B00665 |
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