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Atomistry » Zinc » PDB 6wdv-6wq1 » 6wdx » |
Zinc in PDB 6wdx: Crystal Structure of Danio Rerio Histone Deacetylase 10 in Complex with Hydroxyethylindole Phenylhydroxamate InhibitorEnzymatic activity of Crystal Structure of Danio Rerio Histone Deacetylase 10 in Complex with Hydroxyethylindole Phenylhydroxamate Inhibitor
All present enzymatic activity of Crystal Structure of Danio Rerio Histone Deacetylase 10 in Complex with Hydroxyethylindole Phenylhydroxamate Inhibitor:
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 Hydroxyethylindole Phenylhydroxamate Inhibitor, PDB code: 6wdx
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 6wdx:
The structure of Crystal Structure of Danio Rerio Histone Deacetylase 10 in Complex with Hydroxyethylindole Phenylhydroxamate Inhibitor also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Danio Rerio Histone Deacetylase 10 in Complex with Hydroxyethylindole Phenylhydroxamate Inhibitor
(pdb code 6wdx). 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 Danio Rerio Histone Deacetylase 10 in Complex with Hydroxyethylindole Phenylhydroxamate Inhibitor, PDB code: 6wdx: Zinc binding site 1 out of 1 in 6wdxGo back to![]() ![]()
Zinc binding site 1 out
of 1 in the Crystal Structure of Danio Rerio Histone Deacetylase 10 in Complex with Hydroxyethylindole Phenylhydroxamate Inhibitor
![]() Mono view ![]() Stereo pair view
Reference:
C.J.Herbst-Gervasoni,
R.R.Steimbach,
M.Morgen,
A.K.Miller,
D.W.Christianson.
Structural Basis For the Selective Inhibition of HDAC10, the Cytosolic Polyamine Deacetylase. Acs Chem.Biol. V. 15 2154 2020.
Page generated: Tue Oct 29 09:18:52 2024
ISSN: ESSN 1554-8937 PubMed: 32659072 DOI: 10.1021/ACSCHEMBIO.0C00362 |
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