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Bromine in PDB 3sre: Serum Paraoxonase-1 By Directed Evolution at pH 6.5

Enzymatic activity of Serum Paraoxonase-1 By Directed Evolution at pH 6.5

All present enzymatic activity of Serum Paraoxonase-1 By Directed Evolution at pH 6.5:
3.1.1.2;

Protein crystallography data

The structure of Serum Paraoxonase-1 By Directed Evolution at pH 6.5, PDB code: 3sre 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) 33.54 / 1.99
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 93.653, 93.653, 143.705, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 22

Other elements in 3sre:

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

Calcium (Ca) 2 atoms

Bromine Binding Sites:

The binding sites of Bromine atom in the Serum Paraoxonase-1 By Directed Evolution at pH 6.5 (pdb code 3sre). 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, PDB code: 3sre:

Bromine binding site 1 out of 1 in 3sre

Go back to Bromine Binding Sites List in 3sre
Bromine binding site 1 out of 1 in the Serum Paraoxonase-1 By Directed Evolution at pH 6.5


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br1360

b:28.1
occ:0.65
O A:HOH452 3.0 36.1 1.0
O A:HOH402 3.1 31.6 1.0
N A:GLY301 3.2 26.0 1.0
NH1 A:ARG290 3.3 35.1 1.0
CB A:ASN287 3.6 26.7 1.0
N A:ASN287 3.7 22.8 1.0
CD A:ARG290 3.8 38.0 1.0
CB A:PRO286 3.9 22.8 1.0
CA A:GLY301 3.9 24.4 1.0
CD A:PRO286 4.0 24.0 1.0
CG2 A:VAL34 4.0 31.7 1.0
CG A:PRO286 4.2 23.1 1.0
C A:PRO300 4.2 24.8 1.0
CA A:ASN287 4.2 25.9 1.0
CA A:PRO300 4.3 25.8 1.0
CZ A:ARG290 4.4 43.2 1.0
N A:PRO286 4.4 22.6 1.0
C A:PRO286 4.5 21.1 1.0
O A:HOH453 4.5 45.9 1.0
CA A:PRO286 4.5 22.9 1.0
NE A:ARG290 4.5 38.9 1.0
C A:GLY301 4.5 24.3 1.0
O A:ASN287 4.6 26.9 1.0
CB A:ARG290 4.6 28.2 1.0
CG A:ARG290 4.7 33.4 1.0
CG A:ASN287 4.9 31.9 1.0
O A:HOH401 4.9 24.4 1.0
C A:ASN287 5.0 24.8 1.0
O A:GLY301 5.0 22.0 1.0
O A:PRO299 5.0 29.9 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: Sat Dec 12 02:15:36 2020

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