Bromine in PDB 2ht4: Structure of the Escherichia Coli Clc Chloride Channel Y445W Mutant and Fab Complex

The structure of Structure of the Escherichia Coli Clc Chloride Channel Y445W Mutant and Fab Complex, PDB code: 2ht4 was solved by A.Accardi, S.Lobet, C.Williams, C.Miller, R.Dutzler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 3.20
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	234.007, 95.940, 175.327, 90.00, 133.20, 90.00
R / Rfree (%)	23.9 / 26.1

The binding sites of Bromine atom in the Structure of the Escherichia Coli Clc Chloride Channel Y445W Mutant and Fab Complex (pdb code 2ht4). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 4 binding sites of Bromine where determined in the Structure of the Escherichia Coli Clc Chloride Channel Y445W Mutant and Fab Complex, PDB code: 2ht4:
Jump to Bromine binding site number: 1; 2; 3; 4;

Bromine binding site 1 out of 4 in the Structure of the Escherichia Coli Clc Chloride Channel Y445W Mutant and Fab Complex


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Structure of the Escherichia Coli Clc Chloride Channel Y445W Mutant and Fab Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Br474 b:51.6 occ:1.00 N A:ILE356 3.0 70.6 1.0 CZ2 A:TRP445 3.1 78.0 1.0 N A:PHE357 3.3 63.6 1.0 OG A:SER107 3.3 80.5 1.0 CG2 A:ILE356 3.5 58.3 1.0 OE1 A:GLU148 3.5 83.0 1.0 CA A:GLY355 3.6 79.5 1.0 CD1 A:ILE109 3.6 85.5 1.0 CH2 A:TRP445 3.7 78.0 1.0 C A:GLY355 3.8 81.4 1.0 CD1 A:PHE357 3.8 66.3 1.0 CB A:PHE357 3.9 62.0 1.0 CA A:ILE356 3.9 70.4 1.0 CB A:SER107 4.0 74.4 1.0 CE2 A:TRP445 4.0 78.0 1.0 C A:ILE356 4.1 70.5 1.0 CA A:PHE357 4.1 65.0 1.0 CG1 A:ILE109 4.2 72.1 1.0 CB A:ILE356 4.2 56.1 1.0 CG A:PHE357 4.3 64.3 1.0 NE1 A:TRP445 4.4 78.0 1.0 CD A:GLU148 4.5 85.1 1.0 CB A:ILE109 4.7 73.4 1.0 CE1 A:PHE357 4.8 68.3 1.0 CZ3 A:TRP445 4.9 78.0 1.0 OE2 A:GLU148 5.0 87.7 1.0 N A:GLY355 5.0 80.0 1.0 CA A:GLY149 5.0 65.1 1.0 O A:GLY355 5.0 84.3 1.0

Bromine binding site 2 out of 4 in the Structure of the Escherichia Coli Clc Chloride Channel Y445W Mutant and Fab Complex


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Structure of the Escherichia Coli Clc Chloride Channel Y445W Mutant and Fab Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Br475 b:51.6 occ:1.00 N A:SER107 3.2 69.2 1.0 CA A:GLY106 3.6 73.3 1.0 CZ A:PHE348 3.7 59.2 1.0 C A:GLY106 3.9 72.8 1.0 CG A:PRO110 4.0 84.3 1.0 CB A:SER107 4.1 74.4 1.0 CG2 A:ILE448 4.1 60.4 1.0 CA A:SER107 4.2 70.3 1.0 O A:GLY105 4.3 99.8 1.0 CE2 A:PHE348 4.3 57.5 1.0 CE1 A:PHE348 4.4 59.8 1.0 OE1 A:GLN277 4.4 89.3 1.0 N A:GLY108 4.5 83.9 1.0 N A:GLY106 4.5 76.4 1.0 CD A:PRO110 4.6 85.0 1.0 CG1 A:ILE448 4.6 66.7 1.0 C A:GLY105 4.7 99.6 1.0 C A:SER107 4.9 70.6 1.0

Bromine binding site 3 out of 4 in the Structure of the Escherichia Coli Clc Chloride Channel Y445W Mutant and Fab Complex


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Structure of the Escherichia Coli Clc Chloride Channel Y445W Mutant and Fab Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Br474 b:51.6 occ:1.00 CH2 B:TRP445 2.6 80.6 1.0 N B:ILE356 2.8 49.1 1.0 CG2 B:ILE356 3.2 38.8 1.0 N B:PHE357 3.3 68.5 1.0 CZ2 B:TRP445 3.4 80.6 1.0 CA B:GLY355 3.5 90.3 1.0 OG B:SER107 3.5 70.4 1.0 CZ3 B:TRP445 3.5 80.6 1.0 OE1 B:GLU148 3.6 91.7 1.0 C B:GLY355 3.6 90.7 1.0 CA B:ILE356 3.7 54.7 1.0 C B:ILE356 3.9 56.2 1.0 CD1 B:PHE357 3.9 81.7 1.0 CB B:ILE356 3.9 42.3 1.0 CB B:SER107 3.9 68.4 1.0 CG1 B:ILE109 4.0 44.8 1.0 CB B:PHE357 4.2 78.1 1.0 CA B:PHE357 4.2 69.8 1.0 CG B:PHE357 4.5 81.5 1.0 CE2 B:TRP445 4.7 80.6 1.0 CD1 B:ILE109 4.7 66.2 1.0 CD B:GLU148 4.8 94.9 1.0 CE3 B:TRP445 4.8 80.6 1.0 CA B:SER107 4.8 64.7 1.0 CE1 B:PHE348 4.8 60.9 1.0 O B:GLY355 4.8 88.9 1.0 CE1 B:PHE357 4.8 84.3 1.0 N B:GLY355 4.9 94.0 1.0 CB B:ILE109 4.9 46.2 1.0 O B:ILE356 5.0 58.4 1.0

Bromine binding site 4 out of 4 in the Structure of the Escherichia Coli Clc Chloride Channel Y445W Mutant and Fab Complex


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 4 of Structure of the Escherichia Coli Clc Chloride Channel Y445W Mutant and Fab Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Br475 b:51.6 occ:1.00 N B:SER107 3.0 59.4 1.0 CG B:PRO110 3.2 34.1 1.0 CB B:SER107 3.4 68.4 1.0 CZ B:PHE348 3.7 61.2 1.0 CA B:SER107 3.7 64.7 1.0 CD B:PRO110 3.7 33.1 1.0 N B:GLY108 3.8 69.1 1.0 CG2 B:ILE448 3.8 74.8 1.0 CA B:GLY106 4.0 85.0 1.0 C B:GLY106 4.0 82.7 1.0 CE1 B:PHE348 4.3 60.9 1.0 C B:SER107 4.3 64.7 1.0 O B:GLY105 4.4 82.6 1.0 OG B:SER107 4.5 70.4 1.0 CB B:PRO110 4.5 34.5 1.0 CE2 B:PHE348 4.5 60.3 1.0 CG1 B:ILE448 4.8 82.2 1.0 CB B:ILE448 4.9 82.6 1.0 CA B:GLY108 5.0 69.8 1.0 N B:GLY106 5.0 87.1 1.0

A.Accardi, S.Lobet, C.Williams, C.Miller, R.Dutzler. Synergism Between Halide Binding and Proton Transport in A Clc-Type Exchanger. J.Mol.Biol. V. 362 691 2006.
ISSN: ISSN 0022-2836
PubMed: 16949616
DOI: 10.1016/J.JMB.2006.07.081