Chlorine in PDB 3srg: Serum Paraoxonase-1 By Directed Evolution at pH 6.5 in Complex with 2- Hydroxyquinoline

All present enzymatic activity of Serum Paraoxonase-1 By Directed Evolution at pH 6.5 in Complex with 2- Hydroxyquinoline:
3.1.1.2;

The structure of Serum Paraoxonase-1 By Directed Evolution at pH 6.5 in Complex with 2- Hydroxyquinoline, PDB code: 3srg was solved by M.Ben David, M.Elias, I.Silman, J.L.Sussman, D.S.Tawfik, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.77 / 2.19
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	93.544, 93.544, 144.621, 90.00, 90.00, 90.00
R / Rfree (%)	18.2 / 22.7

The structure of Serum Paraoxonase-1 By Directed Evolution at pH 6.5 in Complex with 2- Hydroxyquinoline also contains other interesting chemical elements:

Bromine	(Br)	1 atom
Calcium	(Ca)	3 atoms

The binding sites of Chlorine atom in the Serum Paraoxonase-1 By Directed Evolution at pH 6.5 in Complex with 2- Hydroxyquinoline (pdb code 3srg). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Serum Paraoxonase-1 By Directed Evolution at pH 6.5 in Complex with 2- Hydroxyquinoline, PDB code: 3srg:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Serum Paraoxonase-1 By Directed Evolution at pH 6.5 in Complex with 2- Hydroxyquinoline


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Serum Paraoxonase-1 By Directed Evolution at pH 6.5 in Complex with 2- Hydroxyquinoline within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1361 b:32.3 occ:1.00 N A:ILE187 3.2 34.0 1.0 N A:ASP188 3.3 38.5 1.0 CB A:ILE187 3.7 36.9 1.0 CA A:ILE187 3.9 36.2 1.0 CB A:ASP188 3.9 40.1 1.0 CD2 A:LEU191 4.0 34.7 1.0 CD1 A:PHE186 4.0 27.6 1.0 C A:ILE187 4.1 37.7 1.0 CB A:PHE186 4.2 27.9 1.0 CA A:ASP188 4.2 38.9 1.0 C A:PHE186 4.2 32.9 1.0 CA A:PHE186 4.4 29.5 1.0 CG1 A:ILE187 4.4 35.5 1.0 CG A:PHE186 4.6 30.7 1.0 CD1 A:ILE187 4.8 35.6 1.0 CG2 A:ILE187 4.9 35.4 1.0

Chlorine binding site 2 out of 2 in the Serum Paraoxonase-1 By Directed Evolution at pH 6.5 in Complex with 2- Hydroxyquinoline


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Serum Paraoxonase-1 By Directed Evolution at pH 6.5 in Complex with 2- Hydroxyquinoline within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1362 b:48.2 occ:1.00 N A:LEU311 3.6 39.8 1.0 CA A:ASP309 3.6 32.3 1.0 C A:ASP309 3.7 32.2 1.0 CB A:LEU311 3.7 43.7 1.0 N A:ILE310 3.8 32.7 1.0 CG A:LEU311 4.0 44.8 1.0 CA A:LEU311 4.1 43.7 1.0 O A:HOH423 4.1 52.5 1.0 CD1 A:LEU311 4.2 45.6 1.0 O A:ASP309 4.3 32.2 1.0 N A:SER312 4.3 47.9 1.0 CB A:ASP309 4.4 34.2 1.0 N A:ASP309 4.6 29.3 1.0 C A:LEU311 4.6 46.2 1.0 C A:ILE310 4.6 36.7 1.0 OD1 A:ASP309 4.7 47.6 1.0 CA A:ILE310 4.8 33.5 1.0 CG A:ASP309 5.0 43.3 1.0

M.Ben-David, M.Elias, J.J.Filippi, E.Dunach, I.Silman, J.L.Sussman, D.S.Tawfik. Catalytic Versatility and Backups in Enzyme Active Sites: the Case of Serum Paraoxonase 1. J.Mol.Biol. V. 418 181 2012.
ISSN: ISSN 0022-2836
PubMed: 22387469
DOI: 10.1016/J.JMB.2012.02.042