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Atomistry » Zinc » PDB 6uat-6uo3 » 6uim » |
Zinc in PDB 6uim: Crystal Structure of Danio Rerio Histone Deacetylase 10 in Complex with 7-{[(3-Aminopropyl)Amino]-2-Oxoheptyl} ThioacetateEnzymatic activity of Crystal Structure of Danio Rerio Histone Deacetylase 10 in Complex with 7-{[(3-Aminopropyl)Amino]-2-Oxoheptyl} Thioacetate
All present enzymatic activity of Crystal Structure of Danio Rerio Histone Deacetylase 10 in Complex with 7-{[(3-Aminopropyl)Amino]-2-Oxoheptyl} Thioacetate:
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 7-{[(3-Aminopropyl)Amino]-2-Oxoheptyl} Thioacetate, PDB code: 6uim
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 6uim:
The structure of Crystal Structure of Danio Rerio Histone Deacetylase 10 in Complex with 7-{[(3-Aminopropyl)Amino]-2-Oxoheptyl} Thioacetate 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 7-{[(3-Aminopropyl)Amino]-2-Oxoheptyl} Thioacetate
(pdb code 6uim). 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 7-{[(3-Aminopropyl)Amino]-2-Oxoheptyl} Thioacetate, PDB code: 6uim: Zinc binding site 1 out of 1 in 6uimGo back to Zinc Binding Sites List in 6uim
Zinc binding site 1 out
of 1 in the Crystal Structure of Danio Rerio Histone Deacetylase 10 in Complex with 7-{[(3-Aminopropyl)Amino]-2-Oxoheptyl} Thioacetate
Mono view Stereo pair view
Reference:
C.J.Herbst-Gervasoni,
D.W.Christianson.
Binding of N8-Acetylspermidine Analogues to Histone Deacetylase 10 Reveals Molecular Strategies For Blocking Polyamine Deacetylation. Biochemistry 2019.
Page generated: Tue Oct 29 08:37:18 2024
ISSN: ISSN 0006-2960 PubMed: 31746596 DOI: 10.1021/ACS.BIOCHEM.9B00906 |
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