Zinc in PDB 7kur: Crystal Structure of Danio Rerio Histone Deacetylase 10 Y307F Mutant in Complex with N-Acetylputrescine

Enzymatic activity of Crystal Structure of Danio Rerio Histone Deacetylase 10 Y307F Mutant in Complex with N-Acetylputrescine

All present enzymatic activity of Crystal Structure of Danio Rerio Histone Deacetylase 10 Y307F Mutant in Complex with N-Acetylputrescine:
3.5.1.48; 3.5.1.62;

Protein crystallography data

The structure of Crystal Structure of Danio Rerio Histone Deacetylase 10 Y307F Mutant in Complex with N-Acetylputrescine, PDB code: 7kur 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:

Resolution Low / High (Å) 69.77 / 2.10
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 80.56, 80.56, 245.71, 90, 90, 120
R / Rfree (%) 19.1 / 21.7

Other elements in 7kur:

The structure of Crystal Structure of Danio Rerio Histone Deacetylase 10 Y307F Mutant in Complex with N-Acetylputrescine also contains other interesting chemical elements:

Potassium (K) 2 atoms
Sodium (Na) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Danio Rerio Histone Deacetylase 10 Y307F Mutant in Complex with N-Acetylputrescine (pdb code 7kur). 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 Y307F Mutant in Complex with N-Acetylputrescine, PDB code: 7kur:

Zinc binding site 1 out of 1 in 7kur

Go back to Zinc Binding Sites List in 7kur
Zinc binding site 1 out of 1 in the Crystal Structure of Danio Rerio Histone Deacetylase 10 Y307F Mutant in Complex with N-Acetylputrescine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Danio Rerio Histone Deacetylase 10 Y307F Mutant in Complex with N-Acetylputrescine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn703

b:33.9
occ:1.00
 OD2 A:ASP174 2.0 27.0 1.0
OD2 A:ASP267 2.1 31.6 1.0
ND1 A:HIS176 2.2 30.6 1.0
O03 A:X5A701 2.2 32.9 1.0
O A:HOH802 2.4 36.8 1.0
OD1 A:ASP174 2.6 29.2 1.0
CG A:ASP174 2.6 32.9 1.0
CG A:ASP267 3.1 27.6 1.0
CE1 A:HIS176 3.1 30.5 1.0
CG A:HIS176 3.2 29.1 1.0
C02 A:X5A701 3.2 37.1 1.0
OD1 A:ASP267 3.3 29.0 1.0
CB A:HIS176 3.5 25.1 1.0
N A:HIS176 3.8 29.1 1.0
C01 A:X5A701 4.1 33.6 1.0
CB A:ASP174 4.1 23.5 1.0
N04 A:X5A701 4.2 39.8 1.0
N A:VAL175 4.2 27.9 1.0
NE2 A:HIS136 4.2 29.6 1.0
NE2 A:HIS176 4.3 32.3 1.0
C05 A:X5A701 4.3 35.0 1.0
CA A:HIS176 4.3 25.9 1.0
CG1 A:VAL175 4.3 28.9 1.0
CD2 A:HIS176 4.3 32.3 1.0
CA A:GLY305 4.3 29.3 1.0
CB A:ASP267 4.4 28.5 1.0
CE2 A:PHE307 4.6 34.6 1.0
NE2 A:HIS137 4.6 32.1 1.0
N A:GLY305 4.6 31.4 1.0
CE1 A:HIS136 4.6 25.6 1.0
C A:VAL175 4.7 31.6 1.0
C A:ASP174 4.8 31.4 1.0
CA A:ASP174 4.9 26.0 1.0
CA A:VAL175 4.9 29.5 1.0
CZ A:PHE307 5.0 34.5 1.0

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.
ISSN: ISSN 0006-2960
PubMed: 33449614
DOI: 10.1021/ACS.BIOCHEM.0C00936
Page generated: Tue Oct 29 22:31:03 2024

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