Chlorine in PDB 5eek: Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 2 in Complex with Trichostatin A

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

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

Protein crystallography data

The structure of Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 2 in Complex with Trichostatin A, PDB code: 5eek 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)*	44.01 / 1.59
*Space group*	P 2₁ 2₁ 2
*Cell size a, b, c (Å), α, β, γ (°)*	83.881, 94.429, 51.698, 90.00, 90.00, 90.00
*R / R_free (%)*	13 / 16.3

Other elements in 5eek:

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

Potassium	(K)	2 atoms
Zinc	(Zn)	1 atom
Iodine	(I)	31 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 2 in Complex with Trichostatin A (pdb code 5eek). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 2 in Complex with Trichostatin A, PDB code: 5eek:

Chlorine binding site 1 out of 1 in 5eek

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Chlorine Binding Sites List in 5eek

Chlorine binding site 1 out of 1 in the Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 2 in Complex with Trichostatin A

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 2 in Complex with Trichostatin A within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl2029 b:45.0 occ:0.51	ND1	A:HIS516	2.4	31.9	1.0
	CE1	A:HIS516	3.1	32.8	1.0
	O	A:LYS512	3.5	13.7	1.0
	CG	A:HIS516	3.6	30.6	1.0
	CB	A:GLU515	3.8	19.0	1.0
	N	A:HIS516	4.0	21.0	1.0
	CB	A:HIS516	4.1	27.5	1.0
	CA	A:SER513	4.2	13.1	1.0
	O	A:SER513	4.2	15.9	1.0
	OE2	A:GLU515	4.3	27.7	1.0
	NE2	A:HIS516	4.3	33.0	1.0
	C	A:SER513	4.4	14.7	1.0
	C	A:LYS512	4.4	13.5	1.0
	CA	A:GLU515	4.5	17.2	1.0
	N	A:GLU515	4.5	15.4	1.0
	C	A:GLU515	4.5	19.0	1.0
	CG	A:GLU515	4.6	22.9	1.0
	CD2	A:HIS516	4.6	32.1	1.0
	CA	A:HIS516	4.7	23.7	1.0
	N	A:SER513	4.8	12.9	1.0
	CG	A:LYS512	4.9	15.7	1.0
	CD	A:GLU515	4.9	26.0	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: Fri Jul 26 07:18:13 2024

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