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Atomistry » Sodium » PDB 7s32-7si5 » 7sgg | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 7s32-7si5 » 7sgg » |
Sodium in PDB 7sgg: Crystal Structure of Danio Rerio Histone Deacetylase 10 in Complex with SahaEnzymatic activity of Crystal Structure of Danio Rerio Histone Deacetylase 10 in Complex with Saha
All present enzymatic activity of Crystal Structure of Danio Rerio Histone Deacetylase 10 in Complex with Saha:
3.5.1.48; 3.5.1.62; Protein crystallography data
The structure of Crystal Structure of Danio Rerio Histone Deacetylase 10 in Complex with Saha, PDB code: 7sgg
was solved by
C.J.Herbst-Gervasoni,
D.W.Christianson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 7sgg:
The structure of Crystal Structure of Danio Rerio Histone Deacetylase 10 in Complex with Saha also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Crystal Structure of Danio Rerio Histone Deacetylase 10 in Complex with Saha
(pdb code 7sgg). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of Danio Rerio Histone Deacetylase 10 in Complex with Saha, PDB code: 7sgg: Sodium binding site 1 out of 1 in 7sggGo back to Sodium Binding Sites List in 7sgg
Sodium binding site 1 out
of 1 in the Crystal Structure of Danio Rerio Histone Deacetylase 10 in Complex with Saha
Mono view Stereo pair view
Reference:
R.R.Steimbach,
C.J.Herbst-Gervasoni,
S.Lechner,
T.M.Stewart,
G.Klinke,
J.Ridinger,
M.N.E.Geraldy,
G.Tihanyi,
J.R.Foley,
U.Uhrig,
B.Kuster,
G.Poschet,
R.A.Casero Jr.,
G.Medard,
I.Oehme,
D.W.Christianson,
N.Gunkel,
A.K.Miller.
Aza-Saha Derivatives Are Selective Histone Deacetylase 10 Chemical Probes That Inhibit Polyamine Deacetylation and Phenocopy HDAC10 Knockout. J.Am.Chem.Soc. V. 144 18861 2022.
Page generated: Wed Oct 9 08:56:56 2024
ISSN: ESSN 1520-5126 PubMed: 36200994 DOI: 10.1021/JACS.2C05030 |
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