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Atomistry » Zinc » PDB 6p3z-6phr » 6pd9 » |
Zinc in PDB 6pd9: Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor 60Enzymatic activity of Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor 60
All present enzymatic activity of Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor 60:
2.3.1.48; Protein crystallography data
The structure of Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor 60, PDB code: 6pd9
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 6pd9:
The structure of Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor 60 also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor 60
(pdb code 6pd9). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor 60, PDB code: 6pd9: Zinc binding site 1 out of 1 in 6pd9Go back to Zinc Binding Sites List in 6pd9
Zinc binding site 1 out
of 1 in the Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor 60
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: Tue Oct 29 04:58:48 2024
ISSN: ISSN 0022-2623 PubMed: 32118427 DOI: 10.1021/ACS.JMEDCHEM.9B02071 |
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