Chlorine in PDB 2xgw: Zinc-Bound Crystal Structure of Streptococcus Pyogenes Dpr

The structure of Zinc-Bound Crystal Structure of Streptococcus Pyogenes Dpr, PDB code: 2xgw was solved by T.Haikarainen, C.-C.Tsou, J.-J.Wu, A.C.Papageorgiou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	107.83 / 2.10
Space group	F 41 3 2
Cell size a, b, c (Å), α, β, γ (°)	187.120, 187.120, 187.120, 90.00, 90.00, 90.00
R / Rfree (%)	14.4 / 17.2

The structure of Zinc-Bound Crystal Structure of Streptococcus Pyogenes Dpr also contains other interesting chemical elements:

Zinc

(Zn)

4 atoms

The binding sites of Chlorine atom in the Zinc-Bound Crystal Structure of Streptococcus Pyogenes Dpr (pdb code 2xgw). 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 Zinc-Bound Crystal Structure of Streptococcus Pyogenes Dpr, PDB code: 2xgw:

Chlorine binding site 1 out of 1 in the Zinc-Bound Crystal Structure of Streptococcus Pyogenes Dpr


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Zinc-Bound Crystal Structure of Streptococcus Pyogenes Dpr within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1179 b:45.8 occ:1.00 ZN A:ZN1178 2.3 35.7 1.0 O A:HOH2025 2.3 50.2 1.0 CD A:LYS99 3.5 30.3 1.0 O A:HOH2184 3.6 32.7 1.0 CG A:GLU96 3.6 17.4 1.0 NE2 A:HIS100 3.7 22.7 1.0 O A:HOH2183 4.0 40.5 1.0 CA A:GLU96 4.0 14.1 1.0 NZ A:LYS99 4.0 36.8 1.0 CD2 A:HIS100 4.0 18.0 1.0 CB A:GLU96 4.3 15.0 1.0 N A:GLU96 4.4 14.2 1.0 CE A:LYS99 4.5 33.8 1.0 CB A:LYS99 4.5 19.4 1.0 O A:ALA95 4.5 15.6 1.0 CG A:LYS99 4.6 22.9 1.0 CD A:GLU96 4.7 20.7 1.0 OE2 A:GLU96 4.7 24.6 1.0 C A:ALA95 4.7 15.2 1.0 CE1 A:HIS100 4.9 22.0 1.0 O A:HOH2092 4.9 10.7 0.5

T.Haikarainen, C.-C.Tsou, J.-J.Wu, A.C.Papageorgiou. Structural Characterization and Biological Implications of Di-Zinc Binding in the Ferroxidase Center of Streptococcus Pyogenes Dpr. Biochem.Biophys.Res.Commun. V. 398 361 2010.
ISSN: ISSN 0006-291X
PubMed: 20599728
DOI: 10.1016/J.BBRC.2010.06.071