Bromine in PDB 4hho: Serum Paraoxonase-1 By Directed Evolution with the H115W Mutation

All present enzymatic activity of Serum Paraoxonase-1 By Directed Evolution with the H115W Mutation:
3.1.1.2; 3.1.1.25; 3.1.8.1;

The structure of Serum Paraoxonase-1 By Directed Evolution with the H115W Mutation, PDB code: 4hho 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)	46.89 / 2.10
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	93.782, 93.782, 145.158, 90.00, 90.00, 90.00
R / Rfree (%)	18.3 / 21.2

The structure of Serum Paraoxonase-1 By Directed Evolution with the H115W Mutation 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 H115W Mutation (pdb code 4hho). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Serum Paraoxonase-1 By Directed Evolution with the H115W Mutation, PDB code: 4hho:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Serum Paraoxonase-1 By Directed Evolution with the H115W Mutation


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 H115W Mutation within 5.0Å range: probe atom residue distance (Å) B Occ A:Br404 b:29.7 occ:0.65 O A:HOH574 3.0 30.9 1.0 O A:HOH503 3.2 34.4 1.0 N A:GLY301 3.2 29.3 1.0 NH1 A:ARG290 3.3 34.8 1.0 CB A:ASN287 3.6 30.8 1.0 N A:ASN287 3.7 26.2 1.0 CD A:ARG290 3.8 37.7 1.0 CA A:GLY301 3.8 25.7 1.0 CB A:PRO286 3.9 20.1 1.0 CG2 A:VAL34 4.0 34.3 1.0 CD A:PRO286 4.1 21.2 1.0 C A:PRO300 4.2 27.4 1.0 CA A:ASN287 4.2 28.5 1.0 CG A:PRO286 4.3 20.4 1.0 CA A:PRO300 4.3 28.8 1.0 CZ A:ARG290 4.3 40.5 1.0 O A:HOH569 4.4 47.1 1.0 N A:PRO286 4.4 21.8 1.0 NE A:ARG290 4.5 37.2 1.0 C A:PRO286 4.5 22.7 1.0 O A:ASN287 4.5 29.4 1.0 C A:GLY301 4.5 26.6 1.0 CA A:PRO286 4.5 22.4 1.0 CG A:ARG290 4.7 33.4 1.0 CB A:ARG290 4.7 29.1 1.0 CG A:ASN287 4.8 39.2 1.0 O A:GLY301 4.9 23.2 1.0 C A:ASN287 4.9 26.6 1.0 CB A:PRO300 4.9 27.4 1.0 O A:HOH506 4.9 24.7 1.0 O A:PRO299 5.0 31.0 1.0

Bromine binding site 2 out of 2 in the Serum Paraoxonase-1 By Directed Evolution with the H115W Mutation


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 H115W Mutation within 5.0Å range: probe atom residue distance (Å) B Occ A:Br405 b:51.2 occ:1.00 N A:ILE187 3.2 31.3 1.0 N A:ASP188 3.3 44.7 1.0 CB A:ILE187 3.8 35.6 1.0 CB A:ASP188 3.8 46.4 1.0 CA A:ILE187 3.9 39.7 1.0 CD1 A:PHE186 3.9 31.6 1.0 CD2 A:LEU191 4.0 35.3 1.0 C A:ILE187 4.1 43.3 1.0 CA A:ASP188 4.2 43.2 1.0 C A:PHE186 4.2 41.0 1.0 CB A:PHE186 4.3 27.9 1.0 CA A:PHE186 4.3 28.7 1.0 CG1 A:ILE187 4.5 35.6 1.0 CG A:PHE186 4.6 30.9 1.0 CE1 A:PHE186 4.9 31.8 1.0 CG2 A:ILE187 5.0 38.2 1.0 CD1 A:ILE187 5.0 37.4 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