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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 3srg:

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

Chlorine (Cl) 2 atoms
Calcium (Ca) 3 atoms

Bromine Binding Sites:

The binding sites of Bromine 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 Bromine atom.
In total only one binding site of Bromine was determined in the Serum Paraoxonase-1 By Directed Evolution at pH 6.5 in Complex with 2- Hydroxyquinoline, PDB code: 3srg:

Bromine binding site 1 out of 1 in 3srg

Go back to Bromine Binding Sites List in 3srg
Bromine binding site 1 out of 1 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 Bromine with other atoms in the Br 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:Br1360

b:0.9
occ:1.00
 OE2 A:GLU148 4.1 60.3 1.0
OD2 A:ASP89 4.2 43.5 1.0
OD1 A:ASN91 4.2 42.9 1.0
O A:ASN60 4.3 32.4 1.0
ND2 A:ASN60 4.3 35.8 1.0
CD2 A:LEU62 4.3 31.6 1.0
CG A:LEU62 4.5 33.1 1.0
CG A:ASN60 4.6 38.1 1.0
OD1 A:ASP89 4.7 38.5 1.0
CG A:ASP89 4.7 36.6 1.0
CB A:ASN60 4.8 34.1 1.0
CD1 A:LEU62 4.9 33.4 1.0

Reference:

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
Page generated: Mon Jul 7 05:55:40 2025

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