Chlorine in PDB 6v2j: Crystal Structure of Clc-EC1 Triple Mutant (E113Q, E148Q, E203Q)

The structure of Crystal Structure of Clc-EC1 Triple Mutant (E113Q, E148Q, E203Q), PDB code: 6v2j was solved by M.Maduke, I.I.Mathews, T.S.Chavan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.65 / 2.62
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	80.970, 120.440, 122.570, 90.00, 90.00, 90.00
R / Rfree (%)	19.3 / 26.2

The binding sites of Chlorine atom in the Crystal Structure of Clc-EC1 Triple Mutant (E113Q, E148Q, E203Q) (pdb code 6v2j). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of Clc-EC1 Triple Mutant (E113Q, E148Q, E203Q), PDB code: 6v2j:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of Clc-EC1 Triple Mutant (E113Q, E148Q, E203Q)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Clc-EC1 Triple Mutant (E113Q, E148Q, E203Q) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl501 b:81.0 occ:1.00 OH A:TYR445 2.9 55.0 1.0 OG A:SER107 3.0 52.7 1.0 N A:ILE356 3.2 51.5 1.0 CA A:GLY355 3.4 59.0 1.0 N A:PHE357 3.7 51.0 1.0 CZ A:TYR445 3.8 46.9 1.0 CB A:SER107 3.8 56.2 1.0 C A:GLY355 3.8 54.7 1.0 N A:GLY149 3.9 49.0 1.0 CL A:CL503 3.9 75.3 1.0 CE1 A:TYR445 4.0 48.0 1.0 CA A:GLY149 4.0 52.2 1.0 CB A:PHE357 4.1 56.7 1.0 NE2 A:GLN148 4.3 68.5 1.0 CA A:ILE356 4.3 53.6 1.0 CG2 A:ILE356 4.4 50.7 1.0 CD1 A:ILE109 4.4 61.1 1.0 C A:ILE356 4.4 56.0 1.0 CA A:SER107 4.5 56.8 1.0 CA A:PHE357 4.5 51.1 1.0 CG A:GLN148 4.6 61.7 1.0 CB A:GLN148 4.6 55.2 1.0 N A:GLY355 4.8 53.4 1.0 CB A:ILE356 4.8 55.0 1.0 CD A:GLN148 4.9 62.8 1.0 C A:GLN148 4.9 53.2 1.0 CE2 A:TYR445 5.0 47.5 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of Clc-EC1 Triple Mutant (E113Q, E148Q, E203Q)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Clc-EC1 Triple Mutant (E113Q, E148Q, E203Q) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl502 b:95.5 occ:1.00 N A:SER107 3.1 55.7 1.0 CG A:PRO110 3.6 52.9 1.0 CB A:SER107 3.7 56.2 1.0 CG2 A:ILE448 3.8 43.6 1.0 CA A:GLY106 3.8 57.1 1.0 CZ A:PHE348 3.9 57.5 1.0 C A:GLY106 3.9 57.9 1.0 CA A:SER107 4.0 56.8 1.0 CD A:PRO110 4.0 53.0 1.0 CD1 A:ILE448 4.1 50.0 1.0 O A:HOH608 4.3 76.9 1.0 CE1 A:PHE348 4.4 61.7 1.0 N A:GLY108 4.5 59.5 1.0 CB A:PRO110 4.6 48.2 1.0 O A:GLY105 4.7 53.4 1.0 CB A:ILE448 4.7 48.1 1.0 CE2 A:PHE348 4.8 57.7 1.0 C A:SER107 4.8 60.3 1.0 CG1 A:ILE448 4.9 52.5 1.0 OG A:SER107 4.9 52.7 1.0 N A:GLY106 5.0 53.2 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of Clc-EC1 Triple Mutant (E113Q, E148Q, E203Q)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Clc-EC1 Triple Mutant (E113Q, E148Q, E203Q) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl503 b:75.3 occ:1.00 C A:GLY146 3.1 64.5 1.0 N A:GLN148 3.1 49.9 1.0 CA A:GLY146 3.3 64.2 1.0 CB A:PHE357 3.3 56.7 1.0 O A:GLY146 3.4 62.4 1.0 N A:ARG147 3.4 59.2 1.0 CA A:GLY355 3.4 59.0 1.0 N A:PHE357 3.5 51.0 1.0 CB A:GLN148 3.5 55.2 1.0 C A:GLY355 3.6 54.7 1.0 CA A:GLN148 3.8 48.5 1.0 N A:ALA358 3.8 51.5 1.0 N A:GLY149 3.8 49.0 1.0 CA A:PHE357 3.9 51.1 1.0 CL A:CL501 3.9 81.0 1.0 N A:GLY146 3.9 58.7 1.0 N A:ILE356 3.9 51.5 1.0 C A:ARG147 4.0 53.3 1.0 O A:GLY355 4.1 54.6 1.0 N A:GLY355 4.2 53.4 1.0 CA A:ARG147 4.3 56.7 1.0 C A:GLN148 4.3 53.2 1.0 C A:PHE357 4.3 51.8 1.0 CG A:PHE357 4.5 58.5 1.0 C A:ILE356 4.5 56.0 1.0 CG A:GLN148 4.7 61.7 1.0 CB A:ALA358 4.7 60.3 1.0 CD2 A:PHE357 4.7 60.1 1.0 CA A:ILE356 4.8 53.6 1.0 CD A:PRO150 4.8 50.9 1.0 CA A:ALA358 4.9 55.0 1.0 CD A:PRO359 4.9 56.4 1.0 O A:ARG147 5.0 60.1 1.0 CA A:GLY149 5.0 52.2 1.0

T.S.Chavan, R.C.Cheng, T.Jiang, I.I.Mathews, R.A.Stein, A.Koehl, H.S.Mchaourab, E.Tajkhorshid, M.Maduke. A Clc-EC1 Mutant Reveals Global Conformational Change and Suggests A Unifying Mechanism For the Cl-/H+Transport Cycle. Elife V. 9 2020.
ISSN: ESSN 2050-084X
PubMed: 32310757
DOI: 10.7554/ELIFE.53479