Chlorine in PDB 5u8o: Crystal Structure of Beta-Lactamase Domain Protein, From Burkholderia Multivorans

The structure of Crystal Structure of Beta-Lactamase Domain Protein, From Burkholderia Multivorans, PDB code: 5u8o was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.10 / 2.40
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	45.520, 106.830, 144.330, 90.00, 91.30, 90.00
R / Rfree (%)	16.3 / 22.2

The structure of Crystal Structure of Beta-Lactamase Domain Protein, From Burkholderia Multivorans also contains other interesting chemical elements:

Zinc	(Zn)	8 atoms
Calcium	(Ca)	1 atom

The binding sites of Chlorine atom in the Crystal Structure of Beta-Lactamase Domain Protein, From Burkholderia Multivorans (pdb code 5u8o). 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 Beta-Lactamase Domain Protein, From Burkholderia Multivorans, PDB code: 5u8o:

Chlorine binding site 1 out of 1 in the Crystal Structure of Beta-Lactamase Domain Protein, From Burkholderia Multivorans


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 Beta-Lactamase Domain Protein, From Burkholderia Multivorans within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl404 b:68.0 occ:1.00 NE B:ARG182 3.6 61.8 1.0 NH2 B:ARG182 3.7 62.8 1.0 CZ3 B:TRP120 3.9 32.2 1.0 O B:ARG183 4.0 34.3 1.0 CZ B:ARG182 4.1 61.8 1.0 OD2 B:ASP188 4.4 44.2 1.0 CH2 B:TRP120 4.5 35.4 1.0 CG B:ARG182 4.7 36.6 1.0 CD B:ARG182 4.7 49.6 1.0 CE3 B:TRP120 4.8 27.9 1.0 CG B:ASP188 5.0 44.5 1.0 O B:HOH594 5.0 48.4 1.0

Seattle Structural Genomics Center For Infectious Disease(Ssgcid), S.L.Delker, D.G.Conrady, D.Lorimer, T.E.Edwards. Crystal Structure of Beta-Lactamase Domain Protein, From Burkholderia Multivorans To Be Published.