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Atomistry » Zinc » PDB 6ofs-6oub » 6oin » |
Zinc in PDB 6oin: Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor Ctx-124143Enzymatic activity of Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor Ctx-124143
All present enzymatic activity of Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor Ctx-124143:
2.3.1.48; Protein crystallography data
The structure of Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor Ctx-124143, PDB code: 6oin
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 6oin:
The structure of Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor Ctx-124143 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 Ctx-124143
(pdb code 6oin). 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 Ctx-124143, PDB code: 6oin: Zinc binding site 1 out of 1 in 6oinGo back to Zinc Binding Sites List in 6oin
Zinc binding site 1 out
of 1 in the Crystal Structure of Myst Acetyltransferase Domain in Complex with Inhibitor Ctx-124143
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 Oct 29 04:24:35 2024
ISSN: ISSN 0022-2623 PubMed: 31256587 DOI: 10.1021/ACS.JMEDCHEM.9B00665 |
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