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Zinc in PDB 5efg: Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 2 in Complex with Acetate

Enzymatic activity of Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 2 in Complex with Acetate

All present enzymatic activity of Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 2 in Complex with Acetate:
3.5.1.98;

Protein crystallography data

The structure of Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 2 in Complex with Acetate, PDB code: 5efg was solved by Y.Hai, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.77 / 2.25
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 75.123, 91.852, 96.206, 90.00, 90.00, 90.00
R / Rfree (%) 21.2 / 23.4

Other elements in 5efg:

The structure of Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 2 in Complex with Acetate also contains other interesting chemical elements:

Potassium (K) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 2 in Complex with Acetate (pdb code 5efg). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 2 in Complex with Acetate, PDB code: 5efg:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 5efg

Go back to Zinc Binding Sites List in 5efg
Zinc binding site 1 out of 2 in the Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 2 in Complex with Acetate


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 2 in Complex with Acetate within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn2001

b:19.3
occ:1.00
OD2 D:ASP705 1.9 13.3 1.0
OD2 D:ASP612 2.0 13.4 1.0
O D:ACT2004 2.1 22.4 1.0
OXT D:ACT2004 2.2 22.5 1.0
ND1 D:HIS614 2.3 14.2 1.0
C D:ACT2004 2.5 22.5 1.0
CG D:ASP612 2.7 12.9 1.0
OD1 D:ASP612 2.7 12.1 1.0
CG D:ASP705 3.0 13.0 1.0
CE1 D:HIS614 3.3 14.5 1.0
CG D:HIS614 3.3 14.4 1.0
OD1 D:ASP705 3.5 13.4 1.0
CB D:HIS614 3.5 13.8 1.0
N D:HIS614 3.8 13.8 1.0
CH3 D:ACT2004 4.0 22.6 1.0
O D:HOH2166 4.1 16.2 1.0
CB D:ASP612 4.2 12.8 1.0
CA D:GLY743 4.2 12.8 1.0
CG1 D:VAL613 4.2 14.4 1.0
CB D:ASP705 4.2 12.7 1.0
N D:VAL613 4.3 13.3 1.0
NE2 D:HIS573 4.3 13.6 1.0
CA D:HIS614 4.3 13.8 1.0
NE2 D:HIS614 4.4 15.2 1.0
CD2 D:HIS614 4.4 15.2 1.0
CE1 D:HIS573 4.5 12.8 1.0
OH D:TYR745 4.6 12.8 1.0
N D:GLY743 4.6 13.0 1.0
NE2 D:HIS574 4.6 14.5 1.0
CE2 D:TYR745 4.7 12.9 1.0
C D:VAL613 4.7 13.8 1.0
C D:ASP612 4.8 13.2 1.0
CA D:ASP612 4.9 12.8 1.0
CA D:VAL613 4.9 13.9 1.0
C D:GLY743 5.0 12.5 1.0

Zinc binding site 2 out of 2 in 5efg

Go back to Zinc Binding Sites List in 5efg
Zinc binding site 2 out of 2 in the Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 2 in Complex with Acetate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 2 in Complex with Acetate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn2001

b:21.2
occ:1.00
OD2 A:ASP705 2.0 14.3 1.0
OD2 A:ASP612 2.0 13.9 1.0
ND1 A:HIS614 2.0 14.4 1.0
O A:ACT2004 2.2 24.1 1.0
OXT A:ACT2004 2.2 24.2 1.0
OD1 A:ASP612 2.6 12.7 1.0
C A:ACT2004 2.6 24.1 1.0
CG A:ASP612 2.6 13.3 1.0
CE1 A:HIS614 2.9 14.4 1.0
CG A:ASP705 3.0 14.0 1.0
CG A:HIS614 3.1 14.7 1.0
OD1 A:ASP705 3.5 14.0 1.0
CB A:HIS614 3.6 14.3 1.0
N A:HIS614 3.8 14.5 1.0
NE2 A:HIS614 4.0 14.9 1.0
CH3 A:ACT2004 4.1 24.0 1.0
CB A:ASP612 4.1 13.1 1.0
CA A:GLY743 4.1 13.5 1.0
NE2 A:HIS573 4.1 12.7 1.0
CD2 A:HIS614 4.2 15.1 1.0
O A:HOH2186 4.2 22.3 1.0
CG1 A:VAL613 4.2 16.2 1.0
CB A:ASP705 4.3 14.1 1.0
CA A:HIS614 4.3 13.9 1.0
N A:VAL613 4.3 15.2 1.0
CE1 A:HIS573 4.4 12.5 1.0
OH A:TYR745 4.4 16.4 1.0
N A:GLY743 4.5 13.3 1.0
NE2 A:HIS574 4.7 14.6 1.0
CE2 A:TYR745 4.7 15.6 1.0
C A:VAL613 4.8 15.3 1.0
C A:ASP612 4.8 14.1 1.0
CA A:ASP612 4.9 13.5 1.0
C A:GLY743 5.0 13.3 1.0
CA A:VAL613 5.0 15.7 1.0

Reference:

Y.Hai, D.W.Christianson. Histone Deacetylase 6 Structure and Molecular Basis of Catalysis and Inhibition. Nat.Chem.Biol. V. 12 741 2016.
ISSN: ESSN 1552-4469
PubMed: 27454933
DOI: 10.1038/NCHEMBIO.2134
Page generated: Sun Oct 27 15:15:04 2024

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