Magnesium in PDB 5ikk: Structure of the Histone Deacetylase CLR3

All present enzymatic activity of Structure of the Histone Deacetylase CLR3:
3.5.1.98;

The structure of Structure of the Histone Deacetylase CLR3, PDB code: 5ikk was solved by C.Brugger, T.Schalch, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.82 / 2.40
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	60.487, 187.259, 142.633, 90.00, 90.00, 90.00
R / Rfree (%)	18.7 / 22.8

The structure of Structure of the Histone Deacetylase CLR3 also contains other interesting chemical elements:

Potassium	(K)	2 atoms
Zinc	(Zn)	2 atoms

The binding sites of Magnesium atom in the Structure of the Histone Deacetylase CLR3 (pdb code 5ikk). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Structure of the Histone Deacetylase CLR3, PDB code: 5ikk:

Magnesium binding site 1 out of 1 in the Structure of the Histone Deacetylase CLR3


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Histone Deacetylase CLR3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg712 b:57.0 occ:1.00 O A:HOH934 2.1 38.9 1.0 O A:HOH906 2.1 31.8 1.0 O A:ASP429 2.1 25.6 1.0 O A:VAL432 2.2 24.6 1.0 O A:PRO427 2.3 24.5 1.0 C A:ASP429 3.3 26.1 1.0 C A:PRO427 3.3 25.0 1.0 H A:VAL432 3.4 28.9 1.0 C A:VAL432 3.4 22.5 1.0 HA A:ALA430 3.6 33.9 1.0 HB A:VAL432 3.7 27.4 1.0 C A:LYS428 3.9 44.2 1.0 HA A:PRO427 3.9 28.6 1.0 OD1 A:ASP433 3.9 30.5 1.0 O A:LYS428 4.0 45.6 1.0 N A:ASP429 4.0 27.3 1.0 HA A:ASP433 4.0 33.1 1.0 N A:VAL432 4.0 24.1 1.0 HA A:LYS428 4.1 54.8 1.0 CA A:VAL432 4.1 22.3 1.0 N A:ALA430 4.2 29.7 1.0 CA A:ALA430 4.2 28.2 1.0 CA A:PRO427 4.2 23.9 1.0 N A:LYS428 4.2 45.6 1.0 C A:ALA430 4.3 27.9 1.0 CA A:ASP429 4.3 27.2 1.0 CA A:LYS428 4.3 45.6 1.0 O A:ALA430 4.3 27.6 1.0 H A:ASP429 4.3 32.7 1.0 CB A:VAL432 4.4 22.9 1.0 N A:ASP433 4.5 28.6 1.0 HG12 A:VAL432 4.7 26.5 1.0 CA A:ASP433 4.7 27.6 1.0 HB2 A:ASP429 4.8 33.3 1.0 CG A:ASP433 4.8 30.1 1.0 O A:ASN426 4.8 38.5 1.0 N A:HIS431 4.9 24.9 1.0 HB3 A:PRO427 4.9 28.4 1.0 HA A:ASP429 5.0 32.6 1.0 H A:ALA430 5.0 35.7 1.0

G.Job, C.Brugger, T.Xu, B.R.Lowe, Y.Pfister, C.Qu, S.Shanker, J.I.Banos Sanz, J.F.Partridge, T.Schalch. Shrec Silences Heterochromatin Via Distinct Remodeling and Deacetylation Modules. Mol.Cell V. 62 207 2016.
ISSN: ISSN 1097-2765
PubMed: 27105116
DOI: 10.1016/J.MOLCEL.2016.03.016