Chlorine in PDB 4uht: Crystal Structure of the Dna Binding Domain of Cpxr From E. Coli

The structure of Crystal Structure of the Dna Binding Domain of Cpxr From E. Coli, PDB code: 4uht was solved by A.E.Mechaly, P.M.A.Alzari, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.60 / 1.15
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	39.119, 39.880, 40.940, 89.80, 75.13, 61.04
R / Rfree (%)	12.8 / 15.6

The binding sites of Chlorine atom in the Crystal Structure of the Dna Binding Domain of Cpxr From E. Coli (pdb code 4uht). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of the Dna Binding Domain of Cpxr From E. Coli, PDB code: 4uht:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of the Dna Binding Domain of Cpxr From E. Coli


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 Dna Binding Domain of Cpxr From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1233 b:9.0 occ:1.00 NE A:ARG205 3.1 8.2 1.0 N A:TRP217 3.2 8.0 1.0 N A:PHE218 3.5 7.2 1.0 NH2 A:ARG205 3.7 8.4 1.0 CB A:PRO216 3.7 10.1 1.0 CZ A:ARG205 3.8 8.3 1.0 CB A:TRP217 3.9 8.1 1.0 CA A:PRO216 3.9 9.8 1.0 CD A:ARG205 3.9 8.4 1.0 CA A:TRP217 3.9 7.3 1.0 CG A:ARG205 3.9 8.5 1.0 C A:PRO216 3.9 8.1 1.0 O A:PHE218 4.0 7.6 1.0 C A:TRP217 4.2 6.8 1.0 CD2 A:PHE218 4.3 7.5 1.0 CA A:PHE218 4.4 7.1 1.0 CD1 A:TRP217 4.5 9.8 1.0 CG A:TRP217 4.6 8.2 1.0 CB A:PHE218 4.6 6.9 1.0 C A:PHE218 4.7 7.5 1.0 O A:HOH2176 4.8 11.6 1.0 CG A:PHE218 4.8 7.3 1.0 CB A:ARG205 4.9 7.5 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of the Dna Binding Domain of Cpxr From E. Coli


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of the Dna Binding Domain of Cpxr From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1233 b:9.3 occ:1.00 NE B:ARG205 3.1 8.2 1.0 N B:TRP217 3.1 8.3 1.0 N B:PHE218 3.5 7.8 1.0 NH2 B:ARG205 3.6 8.9 1.0 CB B:PRO216 3.7 10.5 1.0 CZ B:ARG205 3.8 8.2 1.0 CB B:TRP217 3.8 8.4 1.0 CA B:TRP217 3.9 7.9 1.0 CA B:PRO216 3.9 9.4 1.0 CD B:ARG205 3.9 8.0 1.0 C B:PRO216 3.9 8.4 1.0 CG B:ARG205 4.0 8.3 1.0 O B:PHE218 4.0 7.7 1.0 C B:TRP217 4.2 7.5 1.0 CD2 B:PHE218 4.4 8.5 1.0 CD1 B:TRP217 4.4 10.7 1.0 CA B:PHE218 4.5 7.0 1.0 CG B:TRP217 4.6 9.4 1.0 CB B:PHE218 4.7 8.5 1.0 C B:PHE218 4.7 7.8 1.0 O B:HOH2157 4.8 14.9 1.0 CG B:PHE218 4.9 7.4 1.0

A.E.Mechaly, A.Haouz, N.Sassoon, A.Buschiazzo, J.M.Betton, P.M.Alzari. Conformational Plasticity of the Response Regulator Cpxr, A Key Player in Gammaproteobacteria Virulence and Drug-Resistance. J. Struct. Biol. V. 204 165 2018.
ISSN: ESSN 1095-8657
PubMed: 30086390
DOI: 10.1016/J.JSB.2018.08.001