Bromine in PDB 6ada: Crystal Structure of the E148D Mutant Clc-EC1 in 200MM Bromide

The structure of Crystal Structure of the E148D Mutant Clc-EC1 in 200MM Bromide, PDB code: 6ada was solved by H.-H.Lim, K.Park, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.97 / 3.15
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	232.409, 99.956, 170.811, 90.00, 131.88, 90.00
R / Rfree (%)	23.1 / 29

The binding sites of Bromine atom in the Crystal Structure of the E148D Mutant Clc-EC1 in 200MM Bromide (pdb code 6ada). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 4 binding sites of Bromine where determined in the Crystal Structure of the E148D Mutant Clc-EC1 in 200MM Bromide, PDB code: 6ada:
Jump to Bromine binding site number: 1; 2; 3; 4;

Bromine binding site 1 out of 4 in the Crystal Structure of the E148D Mutant Clc-EC1 in 200MM Bromide


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 E148D Mutant Clc-EC1 in 200MM Bromide within 5.0Å range: probe atom residue distance (Å) B Occ A:Br501 b:0.5 occ:1.00 N A:ARG147 3.1 94.9 1.0 CD A:ARG147 3.4 0.3 1.0 CG A:ARG147 3.4 98.0 1.0 NH1 A:ARG147 3.5 97.6 1.0 CB A:ARG147 3.7 95.8 1.0 CA A:GLY146 3.9 87.2 1.0 C A:GLY146 3.9 93.4 1.0 CA A:ARG147 4.0 91.6 1.0 CB A:ALA358 4.0 93.5 1.0 NE A:ARG147 4.3 0.8 1.0 CZ A:ARG147 4.3 0.0 1.0 CE2 A:PHE317 4.5 0.2 1.0 O A:LEU145 4.6 90.3 1.0 CD2 A:PHE317 4.7 91.8 1.0 CD1 A:LEU139 4.9 99.0 1.0 CZ A:PHE317 5.0 96.0 1.0

Bromine binding site 2 out of 4 in the Crystal Structure of the E148D Mutant Clc-EC1 in 200MM Bromide


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 E148D Mutant Clc-EC1 in 200MM Bromide within 5.0Å range: probe atom residue distance (Å) B Occ A:Br502 b:0.3 occ:1.00 N A:SER107 3.3 0.5 1.0 CG A:PRO110 3.7 0.1 1.0 CB A:SER107 3.9 0.4 1.0 CZ A:PHE348 4.0 99.2 1.0 CG2 A:ILE448 4.0 0.6 1.0 CD A:PRO110 4.0 0.3 1.0 CA A:GLY106 4.1 0.0 1.0 C A:GLY106 4.1 0.1 1.0 CA A:SER107 4.1 0.2 1.0 N A:GLY108 4.1 0.9 1.0 CD1 A:ILE448 4.3 0.3 1.0 CE1 A:PHE348 4.5 0.7 1.0 O A:GLY105 4.6 0.7 1.0 C A:SER107 4.7 0.4 1.0 CB A:PRO110 4.7 99.8 1.0 CE2 A:PHE348 4.7 94.7 1.0 CB A:ILE448 5.0 0.6 1.0 OG A:SER107 5.0 0.8 1.0

Bromine binding site 3 out of 4 in the Crystal Structure of the E148D Mutant Clc-EC1 in 200MM Bromide


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Crystal Structure of the E148D Mutant Clc-EC1 in 200MM Bromide within 5.0Å range: probe atom residue distance (Å) B Occ B:Br501 b:0.1 occ:1.00 NH1 B:ARG147 3.6 99.6 1.0 N B:ARG147 3.8 78.8 1.0 CA B:GLY146 3.9 80.7 1.0 CB B:ALA358 3.9 82.4 1.0 CD B:ARG147 4.0 98.7 1.0 CG B:ARG147 4.1 95.8 1.0 CE2 B:PHE317 4.3 88.9 1.0 C B:GLY146 4.4 77.8 1.0 O B:LEU145 4.5 94.6 1.0 CD2 B:PHE317 4.5 86.8 1.0 CB B:ARG147 4.5 90.5 1.0 CZ B:ARG147 4.6 0.2 1.0 NE B:ARG147 4.7 0.9 1.0 CA B:ARG147 4.8 82.6 1.0 CZ B:PHE317 4.8 84.9 1.0 CA B:GLY315 4.8 0.3 1.0 N B:GLY146 5.0 80.2 1.0

Bromine binding site 4 out of 4 in the Crystal Structure of the E148D Mutant Clc-EC1 in 200MM Bromide


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 4 of Crystal Structure of the E148D Mutant Clc-EC1 in 200MM Bromide within 5.0Å range: probe atom residue distance (Å) B Occ B:Br502 b:0.7 occ:1.00 N B:SER107 3.3 96.6 1.0 CZ B:PHE348 3.6 93.1 1.0 CB B:SER107 3.7 95.4 1.0 CD1 B:ILE448 3.7 87.4 1.0 CG B:PRO110 3.8 89.3 1.0 CD B:PRO110 4.0 95.1 1.0 CA B:SER107 4.0 94.8 1.0 N B:GLY108 4.1 0.3 1.0 C B:GLY106 4.2 99.0 1.0 CE1 B:PHE348 4.2 87.0 1.0 CA B:GLY106 4.2 0.2 1.0 CE2 B:PHE348 4.3 95.1 1.0 CG2 B:ILE448 4.3 0.2 1.0 C B:SER107 4.6 98.3 1.0 OG B:SER107 4.7 0.8 1.0 CG1 B:ILE448 4.9 95.2 1.0 O B:GLY105 4.9 0.1 1.0 CB B:PRO110 4.9 92.1 1.0

K.Park, B.C.Lee, H.H.Lim. Mutation of External Glutamate Residue Reveals A New Intermediate Transport State and Anion Binding Site in A Clc Cl-/H+Antiporter. Proc.Natl.Acad.Sci.Usa V. 116 17345 2019.
ISSN: ESSN 1091-6490
PubMed: 31409705
DOI: 10.1073/PNAS.1901822116