Bromine in PDB 2ciy: Chloroperoxidase Complexed with Cyanide and Dmso

All present enzymatic activity of Chloroperoxidase Complexed with Cyanide and Dmso:
1.11.1.10;

The structure of Chloroperoxidase Complexed with Cyanide and Dmso, PDB code: 2ciy 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)	19.84 / 1.70
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	58.210, 151.030, 101.110, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 20.4

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

Bromine binding site 1 out of 2 in the Chloroperoxidase Complexed with Cyanide and Dmso


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 Cyanide and Dmso within 5.0Å range: probe atom residue distance (Å) B Occ A:Br800 b:21.6 occ:0.40 O A:HOH2254 2.9 23.1 1.0 O A:HOH2122 3.0 39.6 1.0 N A:ALA265 3.3 17.6 1.0 O A:HOH2253 3.6 18.1 1.0 CA A:GLY264 3.7 18.5 1.0 CD A:PRO178 3.9 13.4 1.0 CG A:PRO178 3.9 14.3 1.0 C A:GLY264 4.0 17.6 1.0 CB A:LYS177 4.1 13.1 1.0 CB A:ALA265 4.1 17.5 1.0 CA A:ALA265 4.3 17.6 1.0 CD A:LYS177 4.5 15.4 1.0 CE A:LYS177 4.6 17.6 1.0 O A:HOH2248 4.7 28.4 1.0 O A:PRO263 4.7 19.2 1.0 N A:PRO178 4.7 13.5 1.0 NZ A:LYS177 4.8 18.8 1.0 CG A:LYS177 4.9 14.8 1.0

Bromine binding site 2 out of 2 in the Chloroperoxidase Complexed with Cyanide and Dmso


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 Cyanide and Dmso within 5.0Å range: probe atom residue distance (Å) B Occ A:Br801 b:16.4 occ:0.70 O A:HOH2192 3.3 29.0 1.0 O A:HOH2191 3.3 25.0 1.0 NE2 A:GLN116 3.7 15.2 1.0 CD2 A:LEU167 4.0 16.2 1.0 CA A:GLY117 4.1 14.8 1.0 CG A:GLN116 4.1 12.8 1.0 NZ A:LYS112 4.2 29.7 1.0 CD1 A:LEU167 4.2 16.0 1.0 CD A:GLN116 4.4 13.3 1.0 N A:GLY117 4.4 13.8 1.0 CG A:LEU167 4.5 15.9 1.0 CB A:LEU167 4.6 14.5 1.0 C A:GLN116 4.6 12.9 1.0 O A:GLN116 4.7 13.3 1.0 O A:HOH2195 4.8 23.1 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