Bromine in PDB 2ok9: Prtx-I-Bpb

All present enzymatic activity of Prtx-I-Bpb:
3.1.1.4;

The structure of Prtx-I-Bpb, PDB code: 2ok9 was solved by D.P.Marchi-Salvador, C.A.H.Fernandes, A.M.Soares, M.R.Fontes, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.67 / 2.34
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	38.602, 70.002, 43.787, 90.00, 102.64, 90.00
R / Rfree (%)	22.3 / 25.2

The binding sites of Bromine atom in the Prtx-I-Bpb (pdb code 2ok9). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Prtx-I-Bpb, PDB code: 2ok9:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Prtx-I-Bpb


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Prtx-I-Bpb within 5.0Å range: probe atom residue distance (Å) B Occ A:Br248 b:58.3 occ:1.00 BR A:PBP248 0.0 58.3 1.0 CZ A:PBP248 1.9 48.2 1.0 CE2 A:PBP248 2.8 37.1 1.0 CE1 A:PBP248 2.8 39.8 1.0 O A:HOH251 3.0 34.7 1.0 O A:GLY23 3.6 44.3 1.0 C2 A:IPA202 3.8 70.8 1.0 CA A:GLY23 3.8 40.3 1.0 C A:GLY30 4.0 51.3 1.0 O A:TYR22 4.0 44.3 1.0 O A:GLY30 4.0 47.9 1.0 C A:GLY23 4.1 40.4 1.0 O2 A:IPA202 4.1 66.6 1.0 CA A:GLY30 4.1 51.6 1.0 CD2 A:PBP248 4.1 38.4 1.0 CD1 A:PBP248 4.1 39.6 1.0 C3 A:IPA202 4.3 69.2 1.0 N A:GLY30 4.4 45.0 1.0 N A:VAL31 4.4 54.7 1.0 CG1 A:VAL31 4.5 55.9 1.0 CG2 B:VAL31 4.6 70.4 1.0 CG A:PBP248 4.7 39.6 1.0 C A:CYS29 4.8 44.2 1.0 CG1 B:VAL31 4.8 67.4 1.0 N A:GLY23 4.8 44.0 1.0 C A:TYR22 4.8 42.0 1.0 CA A:VAL31 4.9 57.5 1.0 O A:HOH309 4.9 49.7 1.0 CD2 A:LEU2 5.0 58.1 1.0 O A:CYS29 5.0 45.7 1.0 C1 A:IPA202 5.0 69.4 1.0

Bromine binding site 2 out of 2 in the Prtx-I-Bpb


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Prtx-I-Bpb within 5.0Å range: probe atom residue distance (Å) B Occ B:Br248 b:63.7 occ:1.00 BR B:PBP248 0.0 63.7 1.0 CZ B:PBP248 1.9 59.7 1.0 CE1 B:PBP248 2.9 54.2 1.0 CE2 B:PBP248 2.9 56.1 1.0 O B:HOH255 3.1 40.4 1.0 O B:GLY23 3.4 44.9 1.0 O B:TYR22 3.6 33.3 1.0 C B:GLY30 3.7 56.3 1.0 CA B:GLY23 3.7 37.9 1.0 O B:GLY30 3.9 54.5 1.0 C B:GLY23 3.9 39.1 1.0 N B:VAL31 3.9 58.5 1.0 C3 B:IPA201 4.0 56.6 1.0 CA B:GLY30 4.0 54.7 1.0 O2 B:IPA201 4.0 59.2 1.0 CD1 B:PBP248 4.2 54.8 1.0 CD2 B:PBP248 4.2 53.9 1.0 C2 B:IPA201 4.2 61.3 1.0 N B:GLY30 4.3 46.6 1.0 CA B:VAL31 4.3 63.9 1.0 CG1 A:VAL31 4.4 55.9 1.0 C B:TYR22 4.5 40.1 1.0 N B:GLY23 4.6 40.4 1.0 C B:CYS29 4.7 49.9 1.0 CG2 B:VAL31 4.7 70.4 1.0 CG B:PBP248 4.7 55.0 1.0 O B:CYS29 4.8 53.6 1.0

D.P.Marchi-Salvador, C.A.Fernandes, L.B.Silveira, A.M.Soares, M.R.Fontes. Crystal Structure of A Phospholipase A(2) Homolog Complexed with P-Bromophenacyl Bromide Reveals Important Structural Changes Associated with the Inhibition of Myotoxic Activity. Biochim.Biophys.Acta V.1794 1583 2009.
ISSN: ISSN 0006-3002
PubMed: 19616648
DOI: 10.1016/J.BBAPAP.2009.07.005