Bromine in PDB 6adc: Crystal Structure of the E148A Mutant Clc-EC1 in the Presence of 50MM Bromoacetate

The structure of Crystal Structure of the E148A Mutant Clc-EC1 in the Presence of 50MM Bromoacetate, PDB code: 6adc 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)	34.85 / 3.06
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	233.249, 96.732, 169.779, 90.00, 131.45, 90.00
R / Rfree (%)	22.6 / 27.5

The binding sites of Bromine atom in the Crystal Structure of the E148A Mutant Clc-EC1 in the Presence of 50MM Bromoacetate (pdb code 6adc). 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 E148A Mutant Clc-EC1 in the Presence of 50MM Bromoacetate, PDB code: 6adc:
Jump to Bromine binding site number: 1; 2; 3; 4;

Bromine binding site 1 out of 4 in the Crystal Structure of the E148A Mutant Clc-EC1 in the Presence of 50MM Bromoacetate


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 E148A Mutant Clc-EC1 in the Presence of 50MM Bromoacetate within 5.0Å range: probe atom residue distance (Å) B Occ A:Br501 b:0.6 occ:0.50 BR2 A:BXA501 0.0 0.6 0.5 C1 A:BXA501 1.4 0.1 0.5 O1 A:BXA501 1.4 0.7 0.5 O2 A:BXA501 1.6 0.8 0.5 C2 A:BXA501 1.9 0.5 0.5 C2 A:BXA501 2.7 0.2 0.5 N A:ALA148 3.0 1.0 1.0 C1 A:BXA501 3.2 0.5 0.5 N A:GLY149 3.3 0.5 1.0 CA A:GLY146 3.4 97.9 1.0 CB A:ALA148 3.5 0.1 1.0 CA A:ALA148 3.5 0.1 1.0 C A:GLY146 3.6 1.0 1.0 N A:ARG147 3.6 0.8 1.0 N A:ALA358 3.6 0.9 1.0 O2 A:BXA501 3.7 0.1 0.5 C A:ALA148 3.7 0.7 1.0 CB A:PHE357 3.8 98.4 1.0 C A:ARG147 3.8 0.1 1.0 CB A:ALA358 3.9 84.6 1.0 N A:GLY146 4.2 92.3 1.0 O1 A:BXA501 4.3 0.4 0.5 N A:PHE357 4.3 0.5 1.0 CA A:ARG147 4.3 0.9 1.0 CA A:GLY149 4.4 1.0 1.0 O A:GLY146 4.4 0.5 1.0 CA A:ALA358 4.4 93.9 1.0 CA A:PHE357 4.4 0.9 1.0 BR2 A:BXA501 4.5 0.1 0.5 C A:PHE357 4.5 0.0 1.0 C A:GLY355 4.5 0.8 1.0 CA A:GLY355 4.6 0.3 1.0 N A:ILE356 4.7 0.4 1.0 O A:ARG147 4.7 0.9 1.0 CZ A:PHE190 4.7 85.1 1.0 O A:ALA148 4.8 0.2 1.0 CG A:PHE357 4.8 93.3 1.0 O A:GLY355 4.9 0.8 1.0 CD A:PRO359 4.9 99.4 1.0 N A:GLY355 4.9 0.6 1.0

Bromine binding site 2 out of 4 in the Crystal Structure of the E148A Mutant Clc-EC1 in the Presence of 50MM Bromoacetate


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 E148A Mutant Clc-EC1 in the Presence of 50MM Bromoacetate within 5.0Å range: probe atom residue distance (Å) B Occ A:Br501 b:0.1 occ:0.50 BR2 A:BXA501 0.0 0.1 0.5 O1 A:BXA501 0.9 0.4 0.5 C1 A:BXA501 1.3 0.5 0.5 O2 A:BXA501 1.7 0.1 0.5 C2 A:BXA501 2.0 0.2 0.5 C2 A:BXA501 2.7 0.5 0.5 N A:ILE356 3.1 0.4 1.0 C1 A:BXA501 3.2 0.1 0.5 CA A:GLY355 3.4 0.3 1.0 OH A:TYR445 3.5 0.6 1.0 N A:PHE357 3.7 0.5 1.0 C A:GLY355 3.7 0.8 1.0 OG A:SER107 3.8 0.5 1.0 O1 A:BXA501 3.9 0.7 0.5 CB A:SER107 3.9 0.9 1.0 O2 A:BXA501 3.9 0.8 0.5 CB A:PHE357 4.1 98.4 1.0 CA A:GLY149 4.1 1.0 1.0 CA A:ILE356 4.2 0.7 1.0 CE1 A:TYR445 4.3 0.9 1.0 CD1 A:ILE109 4.3 0.2 1.0 CZ A:TYR445 4.3 0.3 1.0 CG2 A:ILE356 4.4 96.1 1.0 C A:ILE356 4.4 0.4 1.0 BR2 A:BXA501 4.5 0.6 0.5 CA A:SER107 4.5 0.3 1.0 N A:GLY149 4.5 0.5 1.0 CA A:PHE357 4.5 0.9 1.0 N A:GLY355 4.6 0.6 1.0 CB A:ILE356 4.7 0.6 1.0 CG1 A:ILE109 4.7 0.4 1.0 CE1 A:PHE348 4.8 92.2 1.0 O A:GLY355 4.9 0.8 1.0

Bromine binding site 3 out of 4 in the Crystal Structure of the E148A Mutant Clc-EC1 in the Presence of 50MM Bromoacetate


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 E148A Mutant Clc-EC1 in the Presence of 50MM Bromoacetate within 5.0Å range: probe atom residue distance (Å) B Occ B:Br501 b:0.9 occ:0.50 BR2 B:BXA501 0.0 0.9 0.5 O1 B:BXA501 0.8 0.6 0.5 C1 B:BXA501 1.2 0.2 0.5 O2 B:BXA501 1.5 0.6 0.5 C2 B:BXA501 2.0 0.9 0.5 C2 B:BXA501 2.7 0.1 0.5 C1 B:BXA501 3.1 0.0 0.5 N B:ALA148 3.3 93.3 1.0 CA B:GLY146 3.3 1.0 1.0 C B:GLY146 3.4 0.1 1.0 CA B:GLY355 3.5 0.8 1.0 CB B:ALA148 3.6 97.8 1.0 C B:GLY355 3.6 0.3 1.0 N B:ALA358 3.7 0.6 1.0 N B:ARG147 3.8 97.3 1.0 O1 B:BXA501 3.8 0.9 0.5 O B:GLY146 3.9 0.8 1.0 N B:GLY146 3.9 0.8 1.0 O2 B:BXA501 3.9 0.5 0.5 CA B:ALA148 3.9 93.7 1.0 N B:GLY149 3.9 0.6 1.0 N B:PHE357 4.0 0.9 1.0 O B:GLY355 4.0 0.5 1.0 N B:GLY355 4.0 0.0 1.0 N B:ILE356 4.0 0.8 1.0 CB B:PHE357 4.1 0.1 1.0 CB B:ALA358 4.1 94.5 1.0 BR2 B:BXA501 4.3 0.7 0.5 C B:ARG147 4.3 94.4 1.0 C B:ALA148 4.4 99.0 1.0 CA B:PHE357 4.4 0.8 1.0 CA B:ALA358 4.5 99.5 1.0 CD B:PRO359 4.5 0.0 1.0 C B:PHE357 4.5 0.7 1.0 CA B:ARG147 4.6 93.5 1.0 C B:ILE356 4.8 0.8 1.0 CD B:PRO150 4.9 92.9 1.0 CA B:ILE356 4.9 0.9 1.0

Bromine binding site 4 out of 4 in the Crystal Structure of the E148A Mutant Clc-EC1 in the Presence of 50MM Bromoacetate


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 E148A Mutant Clc-EC1 in the Presence of 50MM Bromoacetate within 5.0Å range: probe atom residue distance (Å) B Occ B:Br501 b:0.7 occ:0.50 BR2 B:BXA501 0.0 0.7 0.5 O1 B:BXA501 1.1 0.9 0.5 C1 B:BXA501 1.3 0.0 0.5 O2 B:BXA501 1.3 0.5 0.5 C2 B:BXA501 2.0 0.1 0.5 OH B:TYR445 2.8 0.3 1.0 C2 B:BXA501 2.8 0.9 0.5 C1 B:BXA501 3.2 0.2 0.5 N B:ILE356 3.3 0.8 1.0 CA B:GLY355 3.4 0.8 1.0 OG B:SER107 3.4 0.5 1.0 CB B:SER107 3.5 0.3 1.0 CD1 B:ILE109 3.7 99.0 1.0 CZ B:TYR445 3.8 0.4 1.0 C B:GLY355 3.9 0.3 1.0 N B:PHE357 3.9 0.9 1.0 O1 B:BXA501 3.9 0.6 0.5 O2 B:BXA501 4.0 0.6 0.5 CB B:PHE357 4.1 0.1 1.0 CE1 B:TYR445 4.2 1.0 1.0 CA B:GLY149 4.2 99.3 1.0 CA B:SER107 4.2 0.5 1.0 BR2 B:BXA501 4.3 0.9 0.5 N B:GLY149 4.3 0.6 1.0 CG2 B:ILE356 4.4 87.4 1.0 CA B:ILE356 4.4 0.9 1.0 CG1 B:ILE109 4.6 1.0 1.0 N B:GLY355 4.6 0.0 1.0 C B:ILE356 4.6 0.8 1.0 CA B:PHE357 4.7 0.8 1.0 CE1 B:PHE348 4.8 97.0 1.0 CE2 B:TYR445 4.9 0.6 1.0 CB B:ILE356 4.9 95.2 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