Bromine in PDB 2cix: Chloroperoxidase Complexed with Cyclopentanedione

All present enzymatic activity of Chloroperoxidase Complexed with Cyclopentanedione:
1.11.1.10;

The structure of Chloroperoxidase Complexed with Cyclopentanedione, PDB code: 2cix was solved by K.Kuhnel, W.Blankenfeldt, J.Terner, I.Schlichting, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.73 / 1.8
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	57.440, 150.350, 99.620, 90.00, 90.00, 90.00
R / Rfree (%)	17.8 / 21.7

The structure of Chloroperoxidase Complexed with Cyclopentanedione also contains other interesting chemical elements:

Manganese	(Mn)	1 atom
Iron	(Fe)	1 atom

The binding sites of Bromine atom in the Chloroperoxidase Complexed with Cyclopentanedione (pdb code 2cix). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 3 binding sites of Bromine where determined in the Chloroperoxidase Complexed with Cyclopentanedione, PDB code: 2cix:
Jump to Bromine binding site number: 1; 2; 3;

Bromine binding site 1 out of 3 in the Chloroperoxidase Complexed with Cyclopentanedione


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Chloroperoxidase Complexed with Cyclopentanedione within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1321 b:28.9 occ:0.50 O A:HOH2105 2.9 52.8 1.0 O A:HOH2213 3.0 35.7 1.0 N A:ALA265 3.4 22.3 1.0 O A:HOH2214 3.5 22.6 1.0 CA A:GLY264 3.7 23.1 1.0 CD A:PRO178 3.8 17.0 1.0 CG A:PRO178 3.9 17.2 1.0 CB A:LYS177 4.0 19.8 1.0 C A:GLY264 4.1 22.4 1.0 CB A:ALA265 4.2 22.8 1.0 CD A:LYS177 4.3 21.4 1.0 CA A:ALA265 4.4 22.6 1.0 CE A:LYS177 4.5 22.7 1.0 O A:HOH2207 4.6 39.4 1.0 O A:PRO263 4.6 24.1 1.0 N A:PRO178 4.7 17.4 1.0 CG A:LYS177 4.8 20.9 1.0 NZ A:LYS177 4.8 22.6 1.0 CA A:LYS177 4.9 18.9 1.0 N A:GLY264 5.0 23.8 1.0

Bromine binding site 2 out of 3 in the Chloroperoxidase Complexed with Cyclopentanedione


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Chloroperoxidase Complexed with Cyclopentanedione within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1322 b:34.2 occ:0.40 ND2 A:ASN93 3.1 17.8 1.0 NE A:ARG46 3.2 17.6 1.0 O A:HOH2319 3.3 41.7 1.0 O7 A:NAG1302 3.4 21.9 1.0 CD A:ARG46 3.6 17.7 1.0 CB A:ASN93 3.8 15.4 1.0 CG A:ASN93 3.9 17.5 1.0 C1 A:NAG1302 4.0 20.2 1.0 CG A:ARG46 4.0 16.1 1.0 CG1 A:VAL92 4.0 18.6 1.0 C2 A:NAG1302 4.1 22.2 1.0 O A:VAL92 4.1 13.9 1.0 O5 A:NAG1302 4.1 20.0 1.0 C7 A:NAG1302 4.4 20.4 1.0 CZ A:ARG46 4.4 19.2 1.0 O A:HOH2145 4.4 28.4 1.0 NH2 A:ARG46 4.7 21.3 1.0 N2 A:NAG1302 4.7 18.6 1.0 C A:VAL92 4.7 15.9 1.0 CB A:ARG46 5.0 15.3 1.0

Bromine binding site 3 out of 3 in the Chloroperoxidase Complexed with Cyclopentanedione


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Chloroperoxidase Complexed with Cyclopentanedione within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1323 b:25.7 occ:0.80 O A:HOH2188 3.2 21.1 1.0 CB A:HIS147 4.1 18.3 1.0 O A:HOH2186 4.6 46.6 1.0 CG A:HIS147 4.7 17.6 1.0 ND1 A:HIS147 4.7 14.9 1.0 CD1 A:LEU204 4.8 16.7 1.0 O A:HIS147 4.8 17.8 1.0 N A:HIS147 4.9 18.5 1.0 CA A:HIS147 5.0 18.4 1.0

K.Kuhnel, W.Blankenfeldt, J.Terner, I.Schlichting. Crystal Structures of Chloroperoxidase with Its Bound Substrates and Complexed with Formate, Acetate, and Nitrate. J.Biol.Chem. V. 281 23990 2006.
ISSN: ISSN 0021-9258
PubMed: 16790441
DOI: 10.1074/JBC.M603166200