Bromine in PDB 4hhq: Serum Paraoxonase-1 By Directed Evolution with the H115Q and H134Q Mutations

All present enzymatic activity of Serum Paraoxonase-1 By Directed Evolution with the H115Q and H134Q Mutations:
3.1.1.2; 3.1.1.25; 3.1.8.1;

The structure of Serum Paraoxonase-1 By Directed Evolution with the H115Q and H134Q Mutations, PDB code: 4hhq was solved by B.-D.Moshe, W.Grzegorz, E.Mikael, S.Israel, L.S.Joel, S.T.Dan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.34 / 2.30
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	93.789, 93.789, 144.602, 90.00, 90.00, 90.00
R / Rfree (%)	17.7 / 21.8

The structure of Serum Paraoxonase-1 By Directed Evolution with the H115Q and H134Q Mutations also contains other interesting chemical elements:

Calcium

(Ca)

2 atoms

The binding sites of Bromine atom in the Serum Paraoxonase-1 By Directed Evolution with the H115Q and H134Q Mutations (pdb code 4hhq). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 3 binding sites of Bromine where determined in the Serum Paraoxonase-1 By Directed Evolution with the H115Q and H134Q Mutations, PDB code: 4hhq:
Jump to Bromine binding site number: 1; 2; 3;

Bromine binding site 1 out of 3 in the Serum Paraoxonase-1 By Directed Evolution with the H115Q and H134Q Mutations


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Serum Paraoxonase-1 By Directed Evolution with the H115Q and H134Q Mutations within 5.0Å range: probe atom residue distance (Å) B Occ A:Br404 b:19.8 occ:0.60 O A:HOH561 3.1 19.4 1.0 NH1 A:ARG290 3.2 34.5 1.0 O A:HOH502 3.3 25.2 1.0 N A:GLY301 3.3 22.2 1.0 CB A:ASN287 3.6 21.0 1.0 N A:ASN287 3.7 20.9 1.0 CB A:PRO286 3.8 15.8 1.0 CD A:ARG290 3.8 33.2 1.0 CA A:GLY301 4.0 19.0 1.0 CD A:PRO286 4.0 16.2 1.0 CG2 A:VAL34 4.1 26.2 1.0 CG A:PRO286 4.2 16.3 1.0 CA A:ASN287 4.2 21.2 1.0 CZ A:ARG290 4.2 41.0 1.0 CA A:PRO300 4.2 22.2 1.0 C A:PRO300 4.3 22.7 1.0 O A:ASN287 4.3 21.4 1.0 O A:HOH556 4.4 35.7 1.0 NE A:ARG290 4.5 34.1 1.0 C A:PRO286 4.5 18.0 1.0 N A:PRO286 4.5 17.4 1.0 CA A:PRO286 4.5 17.9 1.0 C A:GLY301 4.6 22.3 1.0 CG A:ARG290 4.7 28.4 1.0 CB A:ARG290 4.7 24.7 1.0 C A:ASN287 4.8 22.0 1.0 O A:HOH505 4.8 18.4 1.0 CG A:ASN287 4.8 28.5 1.0 O A:PRO299 4.9 29.8 1.0 O A:GLY301 4.9 18.3 1.0 CB A:PRO300 4.9 20.7 1.0

Bromine binding site 2 out of 3 in the Serum Paraoxonase-1 By Directed Evolution with the H115Q and H134Q Mutations


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Serum Paraoxonase-1 By Directed Evolution with the H115Q and H134Q Mutations within 5.0Å range: probe atom residue distance (Å) B Occ A:Br405 b:34.8 occ:0.60 N A:ASN324 3.3 23.8 1.0 CA A:GLU323 3.6 25.8 1.0 OD1 A:ASN324 3.6 24.2 1.0 CG A:ASN324 3.7 27.1 1.0 CB A:GLU323 3.7 21.7 1.0 C A:GLU323 4.0 25.9 1.0 ND2 A:ASN324 4.0 25.6 1.0 CG A:PRO36 4.0 35.2 1.0 CB A:ASN324 4.2 22.7 1.0 CB A:PRO36 4.2 32.8 1.0 CA A:ASN324 4.4 22.2 1.0 CA A:PRO36 4.7 29.6 1.0 O A:ALA322 4.8 27.9 1.0 CD A:PRO36 4.8 30.8 1.0 OG1 A:THR326 4.8 38.9 1.0 N A:GLU323 4.9 23.9 1.0

Bromine binding site 3 out of 3 in the Serum Paraoxonase-1 By Directed Evolution with the H115Q and H134Q Mutations


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Serum Paraoxonase-1 By Directed Evolution with the H115Q and H134Q Mutations within 5.0Å range: probe atom residue distance (Å) B Occ A:Br406 b:34.3 occ:0.65 N A:ILE187 3.3 28.7 1.0 N A:ASP188 3.3 40.4 1.0 CB A:ILE187 3.8 33.3 1.0 CA A:ILE187 3.9 33.2 1.0 CB A:ASP188 3.9 42.9 1.0 CD2 A:LEU191 4.0 34.4 1.0 CD1 A:PHE186 4.0 25.8 1.0 C A:ILE187 4.1 40.0 1.0 CB A:PHE186 4.2 25.1 1.0 CA A:ASP188 4.2 39.1 1.0 C A:PHE186 4.3 33.5 1.0 CA A:PHE186 4.3 26.2 1.0 CG1 A:ILE187 4.4 29.2 1.0 CG A:PHE186 4.6 28.1 1.0 CD1 A:ILE187 4.8 28.9 1.0 CE1 A:PHE186 5.0 28.9 1.0 CG2 A:ILE187 5.0 30.0 1.0

M.Ben-David, G.Wieczorek, M.Elias, I.Silman, J.L.Sussman, D.S.Tawfik. Catalytic Metal Ion Rearrangements Underline Promiscuity and Evolvability of A Metalloenzyme. J.Mol.Biol. V. 425 1028 2013.
ISSN: ISSN 0022-2836
PubMed: 23318950
DOI: 10.1016/J.JMB.2013.01.009