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Bromine in PDB 3s8y: Bromide Soaked Structure of An Esterase From the Oil-Degrading Bacterium Oleispira Antarctica

Enzymatic activity of Bromide Soaked Structure of An Esterase From the Oil-Degrading Bacterium Oleispira Antarctica

All present enzymatic activity of Bromide Soaked Structure of An Esterase From the Oil-Degrading Bacterium Oleispira Antarctica:
3.1.1.2;

Protein crystallography data

The structure of Bromide Soaked Structure of An Esterase From the Oil-Degrading Bacterium Oleispira Antarctica, PDB code: 3s8y was solved by P.Petit, A.Dong, O.Kagan, A.Savchenko, A.F.Yakunin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.69 / 2.10
Space group P 2 21 21
Cell size a, b, c (Å), α, β, γ (°) 44.532, 84.451, 88.051, 90.00, 90.00, 90.00
R / Rfree (%) 15.4 / 18.5

Bromine Binding Sites:

The binding sites of Bromine atom in the Bromide Soaked Structure of An Esterase From the Oil-Degrading Bacterium Oleispira Antarctica (pdb code 3s8y). 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 Bromide Soaked Structure of An Esterase From the Oil-Degrading Bacterium Oleispira Antarctica, PDB code: 3s8y:

Bromine binding site 1 out of 1 in 3s8y

Go back to Bromine Binding Sites List in 3s8y
Bromine binding site 1 out of 1 in the Bromide Soaked Structure of An Esterase From the Oil-Degrading Bacterium Oleispira Antarctica


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Bromide Soaked Structure of An Esterase From the Oil-Degrading Bacterium Oleispira Antarctica within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br280

b:65.9
occ:0.75
 O A:HOH434 2.5 42.7 1.0
CB A:SER148 2.7 20.0 1.0
OG A:SER148 2.7 20.0 1.0
N A:LEU55 2.9 8.8 1.0
N A:MET149 3.2 14.8 1.0
CA A:GLY54 3.4 10.0 1.0
CG A:LEU55 3.5 9.7 1.0
CB A:LEU55 3.6 7.9 1.0
C A:GLY54 3.6 10.7 1.0
CB A:MET149 3.7 13.6 1.0
CA A:LEU55 3.8 11.8 1.0
CD1 A:LEU55 3.9 11.2 1.0
CA A:SER148 4.0 30.0 1.0
CA A:MET149 4.1 12.3 1.0
C A:SER148 4.1 30.0 1.0
O A:HIS147 4.2 14.1 1.0
NE2 A:HIS257 4.4 15.9 1.0
O A:HOH451 4.7 41.8 1.0
N A:GLY54 4.7 10.6 1.0
O A:LEU55 4.8 13.1 1.0
O A:GLY54 4.8 9.7 1.0
CZ3 A:TRP182 4.8 14.0 1.0
CD2 A:LEU55 4.9 10.1 1.0
C A:LEU55 4.9 11.9 1.0
N A:SER148 4.9 30.0 1.0
CD2 A:HIS147 4.9 13.7 1.0
C A:HIS147 4.9 15.1 1.0
NE2 A:HIS147 4.9 15.7 1.0

Reference:

S.Lemak, A.Tchigvintsev, P.Petit, R.Flick, A.U.Singer, G.Brown, E.Evdokimova, O.Egorova, C.F.Gonzalez, T.N.Chernikova, M.M.Yakimov, M.Kube, R.Reinhardt, P.N.Golyshin, A.Savchenko, A.F.Yakunin. Structure and Activity of the Cold-Active and Anion-Activated Carboxyl Esterase OLEI01171 From the Oil-Degrading Marine Bacterium Oleispira Antarctica. Biochem.J. V. 445 193 2012.
ISSN: ISSN 0264-6021
PubMed: 22519667
DOI: 10.1042/BJ20112113
Page generated: Sat Dec 12 02:15:21 2020

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