Bromine in PDB 2ciz: Chloroperoxidase Complexed with Acetate

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

The structure of Chloroperoxidase Complexed with Acetate, PDB code: 2ciz 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)	19.78 / 1.3
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	57.460, 150.820, 100.390, 90.00, 90.00, 90.00
R / Rfree (%)	14.8 / 17

The structure of Chloroperoxidase Complexed with Acetate 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 Acetate (pdb code 2ciz). 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 Acetate, PDB code: 2ciz:
Jump to Bromine binding site number: 1; 2; 3;

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


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 Acetate within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1322 b:18.9 occ:0.40 O A:HOH2206 2.9 48.5 1.0 O A:HOH2382 3.1 23.2 1.0 N A:ALA265 3.4 15.0 1.0 O A:HOH2375 3.6 17.0 1.0 CA A:GLY264 3.8 15.8 1.0 CD A:PRO178 3.8 11.3 1.0 CG A:PRO178 3.9 12.2 1.0 O A:HOH2466 4.0 49.8 1.0 CB A:LYS177 4.0 12.2 1.0 C A:GLY264 4.1 15.3 1.0 CB A:ALA265 4.2 15.9 1.0 CD A:LYS177 4.3 14.3 1.0 CA A:ALA265 4.4 15.7 1.0 CE A:LYS177 4.4 14.6 1.0 O A:PRO263 4.6 17.4 1.0 CG A:LYS177 4.7 13.1 1.0 N A:PRO178 4.8 11.3 1.0 O A:HOH2377 4.8 25.4 1.0 NZ A:LYS177 4.8 16.3 1.0 CA A:LYS177 5.0 12.0 1.0 N A:GLY264 5.0 15.9 1.0

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


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 Acetate within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1323 b:14.2 occ:0.60 O A:HOH2309 3.2 14.9 1.0 O A:HOH2334 3.4 23.0 1.0 NE2 A:GLN116 3.6 14.3 1.0 CG A:GLN116 3.9 11.3 1.0 CA A:GLY117 4.0 13.8 1.0 CD2 A:LEU167 4.1 13.4 1.0 CD1 A:LEU167 4.1 13.0 1.0 CD A:GLN116 4.3 12.0 1.0 N A:GLY117 4.4 12.9 1.0 CB A:LEU167 4.4 12.6 1.0 CG A:LEU167 4.5 12.3 1.0 C A:GLN116 4.7 12.3 1.0 O A:GLN116 4.7 12.4 1.0 O A:HOH2308 4.9 20.8 1.0

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


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 Acetate within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1324 b:23.2 occ:0.40 O A:HOH2143 2.5 28.6 1.0 O A:HOH2537 3.0 34.4 1.0 ND2 A:ASN93 3.2 12.1 1.0 NE A:ARG46 3.2 12.6 1.0 O7 A:NAG1302 3.3 13.0 1.0 O A:HOH2534 3.5 25.7 1.0 CD A:ARG46 3.6 12.1 1.0 CB A:ASN93 3.9 10.7 1.0 CG A:ASN93 4.0 10.6 1.0 C1 A:NAG1302 4.0 12.6 1.0 O A:HOH2009 4.0 36.4 1.0 CG1 A:VAL92 4.1 13.0 1.0 CG A:ARG46 4.1 10.5 1.0 C2 A:NAG1302 4.1 12.7 1.0 O A:VAL92 4.2 10.5 1.0 O5 A:NAG1302 4.2 12.3 1.0 CZ A:ARG46 4.3 12.2 1.0 C7 A:NAG1302 4.4 12.8 1.0 NH2 A:ARG46 4.5 12.6 1.0 O A:HOH2283 4.6 21.0 1.0 N2 A:NAG1302 4.7 12.5 1.0 O A:HOH2144 4.7 33.6 1.0 C A:VAL92 4.7 10.3 1.0 O A:HOH2008 4.9 47.3 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