Chlorine in PDB 2rht: Crystal Structure of the S112A Mutant of A C-C Hydrolase, Bphd From Burkholderia Xenovorans LB400, in Complex with 3-Cl Hopda

The structure of Crystal Structure of the S112A Mutant of A C-C Hydrolase, Bphd From Burkholderia Xenovorans LB400, in Complex with 3-Cl Hopda, PDB code: 2rht was solved by S.Bhowmik, J.T.Bolin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	83.33 / 1.70
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	117.774, 117.774, 86.739, 90.00, 90.00, 90.00
R / Rfree (%)	15.3 / 18.9

The structure of Crystal Structure of the S112A Mutant of A C-C Hydrolase, Bphd From Burkholderia Xenovorans LB400, in Complex with 3-Cl Hopda also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Chlorine atom in the Crystal Structure of the S112A Mutant of A C-C Hydrolase, Bphd From Burkholderia Xenovorans LB400, in Complex with 3-Cl Hopda (pdb code 2rht). 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 S112A Mutant of A C-C Hydrolase, Bphd From Burkholderia Xenovorans LB400, in Complex with 3-Cl Hopda, PDB code: 2rht:

Chlorine binding site 1 out of 1 in the Crystal Structure of the S112A Mutant of A C-C Hydrolase, Bphd From Burkholderia Xenovorans LB400, in Complex with 3-Cl Hopda


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 S112A Mutant of A C-C Hydrolase, Bphd From Burkholderia Xenovorans LB400, in Complex with 3-Cl Hopda within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl287 b:25.0 occ:1.00 CLA1 A:C1E287 0.0 25.0 1.0 CA3 A:C1E287 1.8 23.8 1.0 CA2 A:C1E287 2.7 19.4 1.0 CA4 A:C1E287 2.8 20.8 1.0 OA3 A:C1E287 2.9 27.4 1.0 CA5 A:C1E287 3.1 18.1 1.0 CE1 A:PHE239 3.4 14.2 1.0 CD1 A:PHE239 3.5 18.5 1.0 CE1 A:PHE175 3.6 32.7 1.0 CD1 A:LEU156 3.6 33.4 1.0 CD1 A:PHE175 4.0 20.2 1.0 CD2 A:HIS265 4.0 17.3 0.5 CA1 A:C1E287 4.1 29.6 1.0 CA A:GLY43 4.2 15.0 1.0 CE A:MET171 4.4 22.2 0.5 CZ A:PHE239 4.4 14.8 1.0 SD A:MET171 4.4 15.8 0.5 NE2 A:HIS265 4.5 12.5 0.5 CZ A:PHE175 4.5 24.3 1.0 N A:GLY43 4.5 15.5 1.0 CG A:PHE239 4.5 13.6 1.0 CA6 A:C1E287 4.6 18.7 1.0 SD A:MET171 4.6 32.9 0.5 CG A:LEU156 4.7 23.4 1.0 OA2 A:C1E287 4.7 33.0 1.0 CB A:LEU156 4.7 16.1 1.0 OA1 A:C1E287 4.8 25.2 1.0

S.Bhowmik, G.P.Horsman, J.T.Bolin, L.D.Eltis. The Molecular Basis For Inhibition of Bphd, A C-C Bond Hydrolase Involved in Polychlorinated Biphenyls Degradation: Large 3-Substituents Prevent Tautomerization. J.Biol.Chem. V. 282 36377 2007.
ISSN: ISSN 0021-9258
PubMed: 17932031
DOI: 10.1074/JBC.M707035200