Zinc in PDB 5ikj: Structure of CLR2 Bound to the CLR1 C-Terminus

The structure of Structure of CLR2 Bound to the CLR1 C-Terminus, PDB code: 5ikj was solved by Y.Pfister, T.Schalch, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.33 / 2.30
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	103.499, 103.499, 135.090, 90.00, 90.00, 120.00
R / Rfree (%)	21.4 / 24.3

The structure of Structure of CLR2 Bound to the CLR1 C-Terminus also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Zinc atom in the Structure of CLR2 Bound to the CLR1 C-Terminus (pdb code 5ikj). 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 Structure of CLR2 Bound to the CLR1 C-Terminus, PDB code: 5ikj:

Zinc binding site 1 out of 1 in the Structure of CLR2 Bound to the CLR1 C-Terminus


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of CLR2 Bound to the CLR1 C-Terminus within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:47.7 occ:1.00 ND1 A:HIS178 2.1 55.2 1.0 SG A:CYS193 2.2 49.3 1.0 SG A:CYS198 2.4 54.8 1.0 SG A:CYS195 2.4 56.1 1.0 HB3 A:CYS195 2.9 56.0 1.0 CE1 A:HIS178 3.1 58.5 1.0 HB2 A:HIS178 3.1 62.8 1.0 CG A:HIS178 3.1 53.4 1.0 HA A:HIS178 3.1 60.3 1.0 HB2 A:CYS198 3.1 64.2 1.0 HB3 A:CYS193 3.2 57.1 1.0 CB A:CYS195 3.2 46.7 1.0 HE1 A:HIS178 3.2 70.2 1.0 CB A:CYS193 3.3 47.6 1.0 CB A:CYS198 3.4 53.5 1.0 HE2 A:HIS163 3.4 61.9 1.0 CB A:HIS178 3.4 52.3 1.0 H A:CYS195 3.5 67.8 1.0 HB2 A:CYS193 3.6 57.1 1.0 H A:CYS198 3.7 51.4 1.0 CA A:HIS178 3.7 50.2 1.0 HB2 A:CYS195 3.9 56.0 1.0 HZ A:PHE169 4.0 60.6 1.0 HB3 A:CYS198 4.0 64.2 1.0 NE2 A:HIS163 4.1 51.6 1.0 NE2 A:HIS178 4.2 61.4 1.0 N A:CYS195 4.2 56.5 1.0 CA A:CYS195 4.2 53.6 1.0 CD2 A:HIS178 4.2 57.8 1.0 N A:CYS198 4.3 42.9 1.0 HD2 A:HIS163 4.4 59.9 1.0 HB3 A:HIS178 4.4 62.8 1.0 HB3 A:TRP181 4.4 55.7 1.0 N A:HIS178 4.4 47.0 1.0 CA A:CYS198 4.5 48.4 1.0 HE3 A:TRP181 4.6 65.9 1.0 CD2 A:HIS163 4.6 49.9 1.0 CA A:CYS193 4.7 61.2 1.0 H A:HIS178 4.7 56.4 1.0 HB2 A:LEU197 4.7 66.2 1.0 C A:CYS195 4.7 53.4 1.0 O A:CYS195 4.8 55.0 1.0 CZ A:PHE169 4.8 50.5 1.0 CE3 A:TRP181 4.9 55.0 1.0 H A:LEU197 4.9 65.4 1.0 C A:CYS193 4.9 57.1 1.0 HE1 A:PHE169 4.9 67.6 1.0 HE2 A:HIS178 5.0 73.7 1.0 C A:HIS178 5.0 59.0 1.0 HA A:CYS198 5.0 58.0 1.0 HA A:CYS193 5.0 73.4 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