Bromine in PDB 6k5i: Crystal Structure of the E148D/R147A/F317A Mutant Clc-EC1 in the Presence of 20 Mm Nabr

The structure of Crystal Structure of the E148D/R147A/F317A Mutant Clc-EC1 in the Presence of 20 Mm Nabr, PDB code: 6k5i 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)	42.89 / 3.02
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	231.914, 98.826, 170.295, 90.00, 131.88, 90.00
R / Rfree (%)	21 / 26.4

The binding sites of Bromine atom in the Crystal Structure of the E148D/R147A/F317A Mutant Clc-EC1 in the Presence of 20 Mm Nabr (pdb code 6k5i). 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 E148D/R147A/F317A Mutant Clc-EC1 in the Presence of 20 Mm Nabr, PDB code: 6k5i:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Crystal Structure of the E148D/R147A/F317A Mutant Clc-EC1 in the Presence of 20 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 E148D/R147A/F317A Mutant Clc-EC1 in the Presence of 20 Mm Nabr within 5.0Å range: probe atom residue distance (Å) B Occ A:Br501 b:0.2 occ:1.00 N A:SER107 3.0 86.8 1.0 CB A:SER107 3.6 85.4 1.0 CG A:PRO110 3.7 75.1 1.0 CD A:PRO110 3.8 76.9 1.0 CA A:SER107 3.8 87.0 1.0 C A:GLY106 3.9 85.9 1.0 CA A:GLY106 3.9 88.7 1.0 N A:GLY108 3.9 94.4 1.0 CZ A:PHE348 4.0 82.1 1.0 CG2 A:ILE448 4.1 82.8 1.0 C A:SER107 4.4 88.6 1.0 O A:GLY105 4.4 92.1 1.0 CE1 A:PHE348 4.5 79.5 1.0 CD1 A:ILE448 4.5 79.1 1.0 CB A:PRO110 4.8 80.8 1.0 OG A:SER107 4.8 83.5 1.0 CE2 A:PHE348 4.8 77.8 1.0 N A:GLY106 4.9 96.2 1.0 O A:GLY106 5.0 85.1 1.0

Bromine binding site 2 out of 2 in the Crystal Structure of the E148D/R147A/F317A Mutant Clc-EC1 in the Presence of 20 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 E148D/R147A/F317A Mutant Clc-EC1 in the Presence of 20 Mm Nabr within 5.0Å range: probe atom residue distance (Å) B Occ B:Br501 b:0.7 occ:1.00 N B:SER107 3.5 82.0 1.0 CG B:PRO110 3.6 71.2 1.0 CB B:SER107 3.7 76.2 1.0 CZ B:PHE348 3.8 72.2 1.0 CD B:PRO110 3.8 75.3 1.0 CD1 B:ILE448 3.8 75.9 1.0 CG2 B:ILE448 3.9 79.5 1.0 N B:GLY108 4.1 78.3 1.0 CA B:SER107 4.2 72.5 1.0 C B:GLY106 4.4 79.0 1.0 CA B:GLY106 4.5 76.0 1.0 CE1 B:PHE348 4.5 73.0 1.0 CE2 B:PHE348 4.5 69.7 1.0 CB B:PRO110 4.6 73.2 1.0 C B:SER107 4.7 74.9 1.0 O B:GLY105 4.8 82.2 1.0 OG B:SER107 4.8 80.7 1.0 CB B:ILE448 4.8 77.0 1.0 NE2 B:GLN277 4.8 90.2 1.0 CG1 B:ILE448 4.9 75.6 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