Bromine in PDB 6k5d: Crystal Structure of the E148N Mutant Clc-EC1 in Presence of 200 Mm Nabr

The structure of Crystal Structure of the E148N Mutant Clc-EC1 in Presence of 200 Mm Nabr, PDB code: 6k5d was solved by K.Park, H.H.Lim, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.92 / 3.20
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	231.719, 99.324, 171.465, 90.00, 131.92, 90.00
R / Rfree (%)	21.5 / 26.2

The binding sites of Bromine atom in the Crystal Structure of the E148N Mutant Clc-EC1 in Presence of 200 Mm Nabr (pdb code 6k5d). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 8 binding sites of Bromine where determined in the Crystal Structure of the E148N Mutant Clc-EC1 in Presence of 200 Mm Nabr, PDB code: 6k5d:
Jump to Bromine binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Bromine binding site 1 out of 8 in the Crystal Structure of the E148N Mutant Clc-EC1 in Presence of 200 Mm Nabr


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 E148N Mutant Clc-EC1 in Presence of 200 Mm Nabr within 5.0Å range: probe atom residue distance (Å) B Occ A:Br501 b:0.9 occ:1.00 N A:ARG147 3.0 87.1 1.0 CG A:ARG147 3.5 91.0 1.0 CB A:ALA358 3.6 89.3 1.0 CA A:GLY146 3.6 80.9 1.0 CB A:ARG147 3.6 86.8 1.0 CD A:ARG147 3.6 95.8 1.0 NH1 A:ARG147 3.7 82.9 1.0 C A:GLY146 3.7 86.1 1.0 CA A:ARG147 3.9 85.5 1.0 NE A:ARG147 4.6 0.2 1.0 CZ A:ARG147 4.6 98.5 1.0 CE1 A:PHE190 4.6 79.9 1.0 CE2 A:PHE317 4.7 87.9 1.0 O A:LEU145 4.7 79.3 1.0 O A:GLY146 4.8 90.6 1.0 N A:GLY146 4.9 73.3 1.0 N A:ASN148 4.9 83.2 1.0 CD2 A:PHE317 4.9 82.9 1.0 C A:ARG147 4.9 84.2 1.0 BR A:BR502 4.9 0.1 1.0 CZ A:PHE317 4.9 89.1 1.0 CA A:ALA358 5.0 81.0 1.0

Bromine binding site 2 out of 8 in the Crystal Structure of the E148N Mutant Clc-EC1 in Presence of 200 Mm Nabr


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 E148N Mutant Clc-EC1 in Presence of 200 Mm Nabr within 5.0Å range: probe atom residue distance (Å) B Occ A:Br502 b:0.1 occ:1.00 CA A:GLY146 2.9 80.9 1.0 N A:ALA358 3.2 84.9 1.0 CB A:PHE357 3.3 87.5 1.0 N A:PHE357 3.4 84.5 1.0 CB A:ASN148 3.4 85.1 1.0 N A:ASN148 3.5 83.2 1.0 C A:GLY146 3.5 86.1 1.0 N A:GLY146 3.6 73.3 1.0 C A:GLY355 3.7 91.9 1.0 CA A:GLY355 3.7 92.2 1.0 N A:ARG147 3.7 87.1 1.0 CB A:ALA358 3.8 89.3 1.0 CA A:PHE357 3.8 85.1 1.0 N A:ILE356 3.8 89.5 1.0 CA A:ASN148 4.0 83.3 1.0 C A:PHE357 4.0 87.3 1.0 N A:GLY149 4.0 89.9 1.0 O A:GLY355 4.1 90.8 1.0 CA A:ALA358 4.2 81.0 1.0 C A:ILE356 4.2 87.5 1.0 N A:GLY355 4.3 89.3 1.0 BR A:BR503 4.3 0.9 1.0 CD A:PRO359 4.3 87.1 1.0 O A:GLY146 4.4 90.6 1.0 C A:ARG147 4.5 84.2 1.0 C A:ASN148 4.6 85.4 1.0 CA A:ILE356 4.6 87.9 1.0 CG A:PHE357 4.6 85.5 1.0 CG A:ASN148 4.7 83.6 1.0 CA A:ARG147 4.7 85.5 1.0 ND2 A:ASN148 4.9 81.4 1.0 C A:LEU145 4.9 79.8 1.0 BR A:BR501 4.9 0.9 1.0 CZ A:PHE190 5.0 81.7 1.0

Bromine binding site 3 out of 8 in the Crystal Structure of the E148N Mutant Clc-EC1 in Presence of 200 Mm Nabr


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 E148N Mutant Clc-EC1 in Presence of 200 Mm Nabr within 5.0Å range: probe atom residue distance (Å) B Occ A:Br503 b:0.9 occ:1.00 OG A:SER107 2.9 97.6 1.0 OH A:TYR445 2.9 97.0 1.0 N A:ILE356 3.3 89.5 1.0 CA A:GLY355 3.4 92.2 1.0 CB A:SER107 3.7 95.7 1.0 N A:PHE357 3.7 84.5 1.0 CA A:GLY149 3.7 86.0 1.0 N A:GLY149 3.7 89.9 1.0 CD1 A:ILE109 3.8 91.1 1.0 C A:GLY355 3.9 91.9 1.0 CZ A:TYR445 4.0 94.8 1.0 CB A:PHE357 4.2 87.5 1.0 BR A:BR502 4.3 0.1 1.0 CE1 A:TYR445 4.3 92.0 1.0 CG2 A:ILE356 4.3 81.8 1.0 ND2 A:ASN148 4.4 81.4 1.0 CA A:SER107 4.4 97.8 1.0 CD1 A:PHE357 4.4 86.8 1.0 CA A:ILE356 4.5 87.9 1.0 CA A:PHE357 4.5 85.1 1.0 C A:ILE356 4.5 87.5 1.0 CG1 A:ILE109 4.6 89.2 1.0 N A:GLY355 4.7 89.3 1.0 CG A:PHE357 4.8 85.5 1.0 C A:ASN148 4.9 85.4 1.0 CB A:ASN148 4.9 85.1 1.0 CB A:ILE356 5.0 86.5 1.0

Bromine binding site 4 out of 8 in the Crystal Structure of the E148N Mutant Clc-EC1 in Presence of 200 Mm Nabr


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 E148N Mutant Clc-EC1 in Presence of 200 Mm Nabr within 5.0Å range: probe atom residue distance (Å) B Occ A:Br504 b:0.5 occ:1.00 N A:SER107 3.1 94.8 1.0 CA A:GLY106 3.8 93.4 1.0 C A:GLY106 3.8 95.5 1.0 CB A:SER107 3.8 95.7 1.0 CZ A:PHE348 3.9 73.8 1.0 CG A:PRO110 3.9 93.3 1.0 CA A:SER107 3.9 97.8 1.0 N A:GLY108 4.0 97.9 1.0 CD A:PRO110 4.2 96.1 1.0 O A:GLY105 4.3 0.2 1.0 CD1 A:ILE448 4.3 96.7 1.0 CG2 A:ILE448 4.3 93.2 1.0 CE1 A:PHE348 4.5 82.7 1.0 C A:SER107 4.5 99.1 1.0 CE2 A:PHE348 4.6 74.6 1.0 N A:GLY106 4.7 0.4 1.0 C A:GLY105 4.8 0.6 1.0 O A:GLY106 4.9 96.5 1.0 CB A:PRO110 4.9 98.2 1.0

Bromine binding site 5 out of 8 in the Crystal Structure of the E148N Mutant Clc-EC1 in Presence of 200 Mm Nabr


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 5 of Crystal Structure of the E148N Mutant Clc-EC1 in Presence of 200 Mm Nabr within 5.0Å range: probe atom residue distance (Å) B Occ B:Br501 b:0.1 occ:1.00 N B:ARG147 3.5 77.5 1.0 CD B:ARG147 3.5 90.0 1.0 CG B:ARG147 3.7 90.5 1.0 CA B:GLY146 3.8 75.7 1.0 NH1 B:ARG147 3.8 0.4 1.0 CB B:ALA358 3.9 86.1 1.0 CB B:ARG147 4.1 84.1 1.0 C B:GLY146 4.2 73.5 1.0 CE2 B:PHE317 4.3 81.1 1.0 CE1 B:PHE190 4.4 87.9 1.0 CA B:ARG147 4.4 81.1 1.0 NE B:ARG147 4.4 0.9 1.0 CZ B:ARG147 4.6 0.9 1.0 CD2 B:PHE317 4.7 86.0 1.0 CZ B:PHE317 4.8 81.5 1.0 CZ B:PHE190 4.9 85.4 1.0

Bromine binding site 6 out of 8 in the Crystal Structure of the E148N Mutant Clc-EC1 in Presence of 200 Mm Nabr


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 6 of Crystal Structure of the E148N Mutant Clc-EC1 in Presence of 200 Mm Nabr within 5.0Å range: probe atom residue distance (Å) B Occ B:Br502 b:0.7 occ:1.00 CB B:ASN148 3.1 85.0 1.0 N B:ASN148 3.3 81.9 1.0 CA B:GLY146 3.3 75.7 1.0 C B:GLY146 3.4 73.5 1.0 CB B:PHE357 3.5 88.5 1.0 N B:ALA358 3.5 92.9 1.0 CA B:GLY355 3.5 79.9 1.0 CA B:ASN148 3.7 80.1 1.0 C B:GLY355 3.7 81.6 1.0 N B:ARG147 3.8 77.5 1.0 O B:GLY146 3.8 83.5 1.0 N B:GLY146 3.8 73.5 1.0 N B:GLY149 3.9 88.4 1.0 N B:PHE357 4.0 91.0 1.0 CB B:ALA358 4.0 86.1 1.0 O B:GLY355 4.0 85.1 1.0 N B:GLY355 4.1 78.4 1.0 CA B:PHE357 4.1 89.3 1.0 N B:ILE356 4.3 83.5 1.0 C B:PHE357 4.3 93.5 1.0 BR B:BR503 4.3 0.3 1.0 CG B:ASN148 4.4 96.0 1.0 CA B:ALA358 4.4 84.7 1.0 C B:ASN148 4.4 86.1 1.0 C B:ARG147 4.4 80.8 1.0 CD B:PRO359 4.4 83.9 1.0 CZ B:PHE190 4.5 85.4 1.0 ND2 B:ASN148 4.6 90.5 1.0 C B:ILE356 4.7 92.0 1.0 CG B:PHE357 4.7 87.5 1.0 CA B:ARG147 4.7 81.1 1.0

Bromine binding site 7 out of 8 in the Crystal Structure of the E148N Mutant Clc-EC1 in Presence of 200 Mm Nabr


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 7 of Crystal Structure of the E148N Mutant Clc-EC1 in Presence of 200 Mm Nabr within 5.0Å range: probe atom residue distance (Å) B Occ B:Br503 b:0.3 occ:1.00 OH B:TYR445 2.4 1.0 1.0 OG B:SER107 2.8 89.8 1.0 CA B:GLY355 3.1 79.9 1.0 N B:ILE356 3.3 83.5 1.0 CB B:SER107 3.6 87.5 1.0 CZ B:TYR445 3.6 96.0 1.0 C B:GLY355 3.7 81.6 1.0 N B:PHE357 3.7 91.0 1.0 N B:GLY149 3.8 88.4 1.0 CB B:PHE357 3.9 88.5 1.0 CA B:GLY149 3.9 86.7 1.0 CD1 B:ILE109 4.0 98.5 1.0 CE1 B:TYR445 4.3 98.0 1.0 BR B:BR502 4.3 0.7 1.0 CG2 B:ILE356 4.3 73.2 1.0 CA B:ILE356 4.4 87.3 1.0 N B:GLY355 4.4 78.4 1.0 CD1 B:PHE357 4.4 89.1 1.0 CA B:PHE357 4.4 89.3 1.0 ND2 B:ASN148 4.5 90.5 1.0 CE2 B:TYR445 4.5 90.9 1.0 C B:ILE356 4.6 92.0 1.0 CG1 B:ILE109 4.6 95.0 1.0 CG B:PHE357 4.6 87.5 1.0 CA B:SER107 4.8 88.7 1.0 O B:GLY355 4.9 85.1 1.0 C B:ASN148 4.9 86.1 1.0 CB B:ILE356 5.0 79.7 1.0 CB B:ASN148 5.0 85.0 1.0

Bromine binding site 8 out of 8 in the Crystal Structure of the E148N Mutant Clc-EC1 in Presence of 200 Mm Nabr


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 8 of Crystal Structure of the E148N Mutant Clc-EC1 in Presence of 200 Mm Nabr within 5.0Å range: probe atom residue distance (Å) B Occ B:Br504 b:0.1 occ:1.00 N B:SER107 3.4 89.6 1.0 CD1 B:ILE448 3.5 82.6 1.0 CZ B:PHE348 3.5 80.5 1.0 CG B:PRO110 3.8 88.6 1.0 CD B:PRO110 4.1 93.8 1.0 CA B:GLY106 4.1 94.0 1.0 CE1 B:PHE348 4.1 81.1 1.0 CB B:SER107 4.2 87.5 1.0 C B:GLY106 4.2 91.0 1.0 N B:GLY108 4.2 97.7 1.0 CG2 B:ILE448 4.2 94.6 1.0 CA B:SER107 4.3 88.7 1.0 CE2 B:PHE348 4.3 78.0 1.0 NE2 B:GLN277 4.8 0.5 1.0 CG1 B:ILE448 4.8 88.6 1.0 O B:GLY105 4.8 99.8 1.0 CB B:PRO110 4.8 89.5 1.0 C B:SER107 4.8 91.3 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