Bromine in PDB 2ez0: Crystal Structure of the S107A/E148Q/Y445A Mutant of Ecclc, in Complex with A Fab Fragment

The structure of Crystal Structure of the S107A/E148Q/Y445A Mutant of Ecclc, in Complex with A Fab Fragment, PDB code: 2ez0 was solved by S.Lobet, R.Dutzler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.92 / 3.54
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	220.155, 124.032, 149.282, 90.00, 127.97, 90.00
R / Rfree (%)	25.8 / 29.6

The binding sites of Bromine atom in the Crystal Structure of the S107A/E148Q/Y445A Mutant of Ecclc, in Complex with A Fab Fragment (pdb code 2ez0). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Crystal Structure of the S107A/E148Q/Y445A Mutant of Ecclc, in Complex with A Fab Fragment, PDB code: 2ez0:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Crystal Structure of the S107A/E148Q/Y445A Mutant of Ecclc, in Complex with A Fab Fragment


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of the S107A/E148Q/Y445A Mutant of Ecclc, in Complex with A Fab Fragment within 5.0Å range: probe atom residue distance (Å) B Occ B:Br474 b:0.7 occ:1.00 N B:GLY149 3.0 51.3 1.0 N B:ALA358 3.3 48.7 1.0 N B:GLN148 3.3 66.9 1.0 CB B:GLN148 3.3 91.9 1.0 CA B:GLY355 3.3 84.4 1.0 CG B:GLN148 3.4 94.8 1.0 CB B:PHE357 3.5 79.0 1.0 C B:GLY355 3.6 82.8 1.0 CA B:GLY146 3.6 74.0 1.0 C B:GLY146 3.6 73.5 1.0 CA B:GLN148 3.7 66.8 1.0 O B:GLY355 3.7 82.1 1.0 CB B:ALA358 3.8 61.0 1.0 C B:GLN148 3.8 65.5 1.0 N B:PHE357 3.8 90.2 1.0 O B:GLY146 3.9 73.4 1.0 CA B:GLY149 3.9 49.0 1.0 N B:ARG147 4.0 58.5 1.0 CD B:PRO150 4.0 33.1 1.0 CA B:PHE357 4.0 89.1 1.0 N B:GLY355 4.0 86.2 1.0 N B:GLY146 4.1 73.1 1.0 C B:PHE357 4.1 87.0 1.0 CA B:ALA358 4.1 47.9 1.0 N B:ILE356 4.3 69.8 1.0 C B:ARG147 4.4 57.2 1.0 CA B:ARG147 4.7 58.8 1.0 CG B:PHE357 4.7 80.6 1.0 C B:ILE356 4.8 70.6 1.0 CD B:GLN148 4.8 96.4 1.0 CD B:PRO359 4.8 0.3 1.0 N B:PRO150 4.9 71.4 1.0 O B:GLN148 5.0 65.9 1.0 C B:GLY149 5.0 47.9 1.0

Bromine binding site 2 out of 2 in the Crystal Structure of the S107A/E148Q/Y445A Mutant of Ecclc, in Complex with A Fab Fragment


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Crystal Structure of the S107A/E148Q/Y445A Mutant of Ecclc, in Complex with A Fab Fragment within 5.0Å range: probe atom residue distance (Å) B Occ A:Br474 b:0.2 occ:1.00 N A:ALA358 2.9 59.8 1.0 CB A:PHE357 3.3 96.1 1.0 N A:GLY149 3.3 75.5 1.0 CA A:GLY355 3.4 83.4 1.0 N A:PHE357 3.4 73.1 1.0 C A:GLY355 3.5 82.8 1.0 CG A:GLN148 3.5 97.9 1.0 CB A:GLN148 3.5 97.2 1.0 CB A:ALA358 3.5 0.7 1.0 O A:GLY355 3.6 83.4 1.0 CA A:GLY146 3.6 0.1 1.0 CA A:PHE357 3.7 73.6 1.0 N A:GLN148 3.7 73.7 1.0 C A:GLY146 3.7 0.3 1.0 C A:PHE357 3.7 72.7 1.0 CA A:ALA358 3.8 59.6 1.0 CA A:GLN148 4.0 71.5 1.0 N A:GLY146 4.0 0.2 1.0 N A:ILE356 4.1 60.4 1.0 O A:GLY146 4.1 0.1 1.0 C A:GLN148 4.1 69.3 1.0 N A:GLY355 4.1 84.2 1.0 N A:ARG147 4.2 84.8 1.0 CA A:GLY149 4.2 73.7 1.0 CD A:PRO150 4.3 73.6 1.0 C A:ILE356 4.5 59.7 1.0 CD A:PRO359 4.5 71.3 1.0 CG A:PHE357 4.6 98.0 1.0 C A:ARG147 4.8 82.8 1.0 CA A:ILE356 4.9 59.8 1.0 CD A:GLN148 4.9 98.2 1.0 O A:PHE357 4.9 72.8 1.0

S.Lobet, R.Dutzler. Ion-Binding Properties of the Clc Chloride Selectivity Filter. Embo J. V. 25 24 2006.
ISSN: ISSN 0261-4189
PubMed: 16341087
DOI: 10.1038/SJ.EMBOJ.7600909