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Zinc in PDB 6uoc: Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 1 (CD1) K330L Mutant Complexed with Givinostat

Protein crystallography data

The structure of Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 1 (CD1) K330L Mutant Complexed with Givinostat, PDB code: 6uoc was solved by J.D.Osko, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.95 / 1.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 55.160, 60.400, 122.160, 90.00, 90.00, 90.00
R / Rfree (%) 15.2 / 16.8

Other elements in 6uoc:

The structure of Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 1 (CD1) K330L Mutant Complexed with Givinostat also contains other interesting chemical elements:

Potassium (K) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 1 (CD1) K330L Mutant Complexed with Givinostat (pdb code 6uoc). 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 6 Catalytic Domain 1 (CD1) K330L Mutant Complexed with Givinostat, PDB code: 6uoc:

Zinc binding site 1 out of 1 in 6uoc

Go back to Zinc Binding Sites List in 6uoc
Zinc binding site 1 out of 1 in the Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 1 (CD1) K330L Mutant Complexed with Givinostat


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 6 Catalytic Domain 1 (CD1) K330L Mutant Complexed with Givinostat within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn604

b:7.7
occ:0.86
H311 A:QCM607 1.9 17.7 1.0
O31 A:QCM607 2.0 14.8 1.0
OD1 A:ASP230 2.0 8.2 1.0
OD2 A:ASP323 2.0 8.8 1.0
ND1 A:HIS232 2.1 8.7 1.0
O01 A:QCM607 2.3 15.4 1.0
N30 A:QCM607 2.5 20.3 1.0
C02 A:QCM607 2.7 18.4 1.0
CG A:ASP230 2.7 6.8 1.0
OD2 A:ASP230 2.8 9.0 1.0
CE1 A:HIS232 3.0 9.4 1.0
CG A:ASP323 3.0 9.1 1.0
CG A:HIS232 3.2 6.5 1.0
H301 A:QCM607 3.3 24.4 1.0
OD1 A:ASP323 3.4 9.0 1.0
CB A:HIS232 3.6 8.0 1.0
N A:HIS232 3.9 6.8 1.0
C03 A:QCM607 4.0 13.9 1.0
CA A:GLY361 4.2 7.3 1.0
NE2 A:HIS232 4.2 8.9 1.0
CB A:ASP230 4.2 7.8 1.0
NE2 A:HIS192 4.2 10.8 1.0
CD2 A:HIS232 4.3 7.4 1.0
CG1 A:VAL231 4.3 8.2 1.0
H291 A:QCM607 4.4 15.8 1.0
CB A:ASP323 4.4 8.2 1.0
N A:VAL231 4.4 7.1 1.0
CA A:HIS232 4.4 6.5 1.0
OH A:TYR363 4.5 14.8 1.0
N A:GLY361 4.5 7.7 1.0
CE2 A:TYR363 4.6 10.2 1.0
C29 A:QCM607 4.6 13.2 1.0
CE1 A:HIS192 4.6 9.7 1.0
NE2 A:HIS193 4.7 9.2 1.0
C A:VAL231 4.8 7.8 1.0
C A:ASP230 4.9 7.1 1.0
CA A:ASP230 4.9 6.7 1.0
C A:GLY361 5.0 7.2 1.0

Reference:

J.D.Osko, D.W.Christianson. Structural Basis of Catalysis and Inhibition of HDAC6 CD1, the Enigmatic Catalytic Domain of Histone Deacetylase 6. Biochemistry 2019.
ISSN: ISSN 0006-2960
PubMed: 31755702
DOI: 10.1021/ACS.BIOCHEM.9B00934
Page generated: Tue Oct 29 08:42:38 2024

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