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Sodium in PDB 7kut: Crystal Structure of Danio Rerio Histone Deacetylase 10 H137A Mutant in Complex with N-Acetylputrescine (Tetrahedral Intermediate)Enzymatic activity of Crystal Structure of Danio Rerio Histone Deacetylase 10 H137A Mutant in Complex with N-Acetylputrescine (Tetrahedral Intermediate)
All present enzymatic activity of Crystal Structure of Danio Rerio Histone Deacetylase 10 H137A Mutant in Complex with N-Acetylputrescine (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 N-Acetylputrescine (Tetrahedral Intermediate), PDB code: 7kut
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 7kut:
The structure of Crystal Structure of Danio Rerio Histone Deacetylase 10 H137A Mutant in Complex with N-Acetylputrescine (Tetrahedral Intermediate) 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 H137A Mutant in Complex with N-Acetylputrescine (Tetrahedral Intermediate)
(pdb code 7kut). 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 H137A Mutant in Complex with N-Acetylputrescine (Tetrahedral Intermediate), PDB code: 7kut: Sodium binding site 1 out of 1 in 7kutGo back to Sodium Binding Sites List in 7kut
Sodium binding site 1 out
of 1 in the Crystal Structure of Danio Rerio Histone Deacetylase 10 H137A Mutant in Complex with N-Acetylputrescine (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: Wed Mar 3 15:35:23 2021
ISSN: ISSN 0006-2960 PubMed: 33449614 DOI: 10.1021/ACS.BIOCHEM.0C00936 |
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