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Zinc in PDB 6ct2: Myst Histone Acetyltransferase KAT6A/B in Complex with Wm-1119Enzymatic activity of Myst Histone Acetyltransferase KAT6A/B in Complex with Wm-1119
All present enzymatic activity of Myst Histone Acetyltransferase KAT6A/B in Complex with Wm-1119:
2.3.1.48; Protein crystallography data
The structure of Myst Histone Acetyltransferase KAT6A/B in Complex with Wm-1119, PDB code: 6ct2
was solved by
B.Ren,
T.S.Peat,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6ct2:
The structure of Myst Histone Acetyltransferase KAT6A/B in Complex with Wm-1119 also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Myst Histone Acetyltransferase KAT6A/B in Complex with Wm-1119
(pdb code 6ct2). 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 Myst Histone Acetyltransferase KAT6A/B in Complex with Wm-1119, PDB code: 6ct2: Zinc binding site 1 out of 1 in 6ct2Go back to Zinc Binding Sites List in 6ct2
Zinc binding site 1 out
of 1 in the Myst Histone Acetyltransferase KAT6A/B in Complex with Wm-1119
Mono view Stereo pair view
Reference:
J.B.Baell,
D.J.Leaver,
S.J.Hermans,
G.L.Kelly,
M.S.Brennan,
N.L.Downer,
N.Nguyen,
J.Wichmann,
H.M.Mcrae,
Y.Yang,
B.Cleary,
H.R.Lagiakos,
S.Mieruszynski,
G.Pacini,
H.K.Vanyai,
M.I.Bergamasco,
R.E.May,
B.K.Davey,
K.J.Morgan,
A.J.Sealey,
B.Wang,
N.Zamudio,
S.Wilcox,
A.L.Garnham,
B.N.Sheikh,
B.J.Aubrey,
K.Doggett,
M.C.Chung,
M.De Silva,
J.Bentley,
P.Pilling,
M.Hattarki,
O.Dolezal,
M.L.Dennis,
H.Falk,
B.Ren,
S.A.Charman,
K.L.White,
J.Rautela,
A.Newbold,
E.D.Hawkins,
R.W.Johnstone,
N.D.Huntington,
T.S.Peat,
J.K.Heath,
A.Strasser,
M.W.Parker,
G.K.Smyth,
I.P.Street,
B.J.Monahan,
A.K.Voss,
T.Thomas.
Inhibitors of Histone Acetyltransferases KAT6A/B Induce Senescence and Arrest Tumour Growth. Nature V. 560 253 2018.
Page generated: Wed Dec 16 11:37:55 2020
ISSN: ESSN 1476-4687 PubMed: 30069049 DOI: 10.1038/S41586-018-0387-5 |
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