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Zinc in PDB 7kus: Crystal Structure of Danio Rerio Histone Deacetylase 10 H137A Mutant in Complex with N8-Acetylspermidine (Tetrahedral Intermediate)Enzymatic activity of Crystal Structure of Danio Rerio Histone Deacetylase 10 H137A Mutant in Complex with N8-Acetylspermidine (Tetrahedral Intermediate)
All present enzymatic activity of Crystal Structure of Danio Rerio Histone Deacetylase 10 H137A Mutant in Complex with N8-Acetylspermidine (Tetrahedral Intermediate):
3.5.1.48; 3.5.1.62; Protein crystallography data
The structure of Crystal Structure of Danio Rerio Histone Deacetylase 10 H137A Mutant in Complex with N8-Acetylspermidine (Tetrahedral Intermediate), PDB code: 7kus
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 7kus:
The structure of Crystal Structure of Danio Rerio Histone Deacetylase 10 H137A Mutant in Complex with N8-Acetylspermidine (Tetrahedral Intermediate) 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 H137A Mutant in Complex with N8-Acetylspermidine (Tetrahedral Intermediate)
(pdb code 7kus). 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 H137A Mutant in Complex with N8-Acetylspermidine (Tetrahedral Intermediate), PDB code: 7kus: Zinc binding site 1 out of 1 in 7kusGo back to Zinc Binding Sites List in 7kus
Zinc binding site 1 out
of 1 in the Crystal Structure of Danio Rerio Histone Deacetylase 10 H137A Mutant in Complex with N8-Acetylspermidine (Tetrahedral Intermediate)
Mono view Stereo pair view
Reference:
C.J.Herbst-Gervasoni,
D.W.Christianson.
X-Ray Crystallographic Snapshots of Substrate Binding in the Active Site of Histone Deacetylase 10. Biochemistry 2021.
Page generated: Tue Oct 29 22:31:03 2024
ISSN: ISSN 0006-2960 PubMed: 33449614 DOI: 10.1021/ACS.BIOCHEM.0C00936 |
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