Chlorine in PDB 6qsz: Crystal Structure of the SIR4 H-Brct Domain in Complex with ESC1 PS1450 Peptide

The structure of Crystal Structure of the SIR4 H-Brct Domain in Complex with ESC1 PS1450 Peptide, PDB code: 6qsz 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)	46.58 / 2.50
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	65.060, 68.340, 77.810, 72.61, 84.10, 87.41
R / Rfree (%)	18.9 / 23.4

The binding sites of Chlorine atom in the Crystal Structure of the SIR4 H-Brct Domain in Complex with ESC1 PS1450 Peptide (pdb code 6qsz). 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 in Complex with ESC1 PS1450 Peptide, PDB code: 6qsz:

Chlorine binding site 1 out of 1 in the Crystal Structure of the SIR4 H-Brct Domain in Complex with ESC1 PS1450 Peptide


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 in Complex with ESC1 PS1450 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl1101 b:95.1 occ:1.00 O G:HOH1123 3.2 39.4 1.0 O C:ASP991 3.4 54.0 1.0 CD1 C:PHE993 3.6 42.7 1.0 O C:HOH1204 3.6 43.4 1.0 O C:HOH1225 3.7 62.4 1.0 CA G:ALA1023 3.7 39.4 1.0 CB G:ALA1023 3.7 39.4 1.0 O G:HOH1104 3.7 47.4 1.0 O G:SER1022 3.8 41.0 1.0 CE1 C:PHE993 3.8 42.8 1.0 N G:ALA1023 3.8 39.6 1.0 C G:SER1022 3.9 42.4 1.0 O G:LYS1021 3.9 49.0 1.0 C C:ASP991 4.3 52.7 1.0 O C:HOH1227 4.5 52.2 1.0 O G:HOH1126 4.5 64.0 1.0 C G:LYS1021 4.8 48.9 1.0 CA C:GLU992 4.8 48.8 1.0 O C:HOH1228 4.8 51.5 1.0 CA G:SER1022 4.9 40.2 1.0 CG C:PHE993 4.9 42.4 1.0 N C:GLU992 4.9 48.0 1.0 N C:PHE993 5.0 44.9 1.0 NZ C:LYS1037 5.0 38.1 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