Chlorine in PDB 6rrv: Crystal Structure of the SIR4 H-Brct Domain

The structure of Crystal Structure of the SIR4 H-Brct Domain, PDB code: 6rrv was solved by I.Deshpande, J.J.Keusch, K.Challa, V.Iesmantavicius, S.M.Gasser, H.Gut, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.89 / 1.10
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	69.660, 38.130, 48.620, 90.00, 118.09, 90.00
R / Rfree (%)	11.7 / 14.2

The structure of Crystal Structure of the SIR4 H-Brct Domain also contains other interesting chemical elements:

Bromine

(Br)

1 atom

The binding sites of Chlorine atom in the Crystal Structure of the SIR4 H-Brct Domain (pdb code 6rrv). 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 the SIR4 H-Brct Domain, PDB code: 6rrv:

Chlorine binding site 1 out of 1 in the Crystal Structure of the SIR4 H-Brct Domain


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 the SIR4 H-Brct Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1101 b:11.5 occ:1.00 HH21 A:ARG1075 2.5 14.6 0.5 O A:HOH1211 3.1 17.8 1.0 HE3 A:LYS1072 3.2 12.4 1.0 O A:HOH1293 3.2 13.0 1.0 HG3 A:LYS1072 3.3 10.8 1.0 NH2 A:ARG1075 3.3 12.1 0.5 HE A:ARG1075 3.4 14.1 0.5 HH22 A:ARG1075 3.8 14.6 0.5 NE A:ARG1075 4.1 11.8 0.5 CE A:LYS1072 4.1 10.3 1.0 CZ A:ARG1075 4.2 11.5 0.5 CG A:LYS1072 4.2 9.0 1.0 O A:HOH1323 4.3 16.0 1.0 HD2 A:LYS1072 4.3 11.1 1.0 CD A:LYS1072 4.4 9.3 1.0 HZ3 A:LYS1072 4.6 15.6 1.0 HG2 A:LYS1072 4.6 10.8 1.0 HE2 A:LYS1072 4.7 12.4 1.0 NZ A:LYS1072 4.8 13.0 1.0 HZ2 A:LYS1072 4.9 15.6 1.0 HA A:LYS1072 5.0 9.2 1.0

I.Deshpande, J.J.Keusch, K.Challa, V.Iesmantavicius, S.M.Gasser, H.Gut. The SIR4 H-Brct Domain Interacts with Phospho-Proteins to Sequester and Repress Yeast Heterochromatin. Embo J. V. 38 01744 2019.
ISSN: ESSN 1460-2075
PubMed: 31515872
DOI: 10.15252/EMBJ.2019101744