Chlorine in PDB 8ta4: Cryo-Em Structure of the Human Clc-2 Chloride Channel Transmembrane Domain with Symmetric C-Terminal

The binding sites of Chlorine atom in the Cryo-Em Structure of the Human Clc-2 Chloride Channel Transmembrane Domain with Symmetric C-Terminal (pdb code 8ta4). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Cryo-Em Structure of the Human Clc-2 Chloride Channel Transmembrane Domain with Symmetric C-Terminal, PDB code: 8ta4:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Cryo-Em Structure of the Human Clc-2 Chloride Channel Transmembrane Domain with Symmetric C-Terminal


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Cryo-Em Structure of the Human Clc-2 Chloride Channel Transmembrane Domain with Symmetric C-Terminal within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl901 b:20.0 occ:1.00 H A:LYS204 2.3 44.0 1.0 H A:MET460 2.7 38.0 1.0 H A:GLU205 3.0 40.0 1.0 HG2 A:MET460 3.0 48.0 1.0 HB3 A:PHE459 3.1 42.0 1.0 HB2 A:MET460 3.2 54.0 1.0 HA3 A:GLY203 3.2 28.0 1.0 N A:LYS204 3.3 44.0 1.0 HB3 A:GLU205 3.4 70.0 1.0 HA2 A:GLY203 3.4 28.0 1.0 HG3 A:MET460 3.5 48.0 1.0 HE1 A:PHE252 3.6 54.0 1.0 CG A:MET460 3.6 48.0 1.0 N A:MET460 3.6 38.0 1.0 HG3 A:LYS204 3.6 34.0 1.0 N A:GLU205 3.7 40.0 1.0 CA A:GLY203 3.7 28.0 1.0 HG2 A:LYS204 3.8 34.0 1.0 CB A:MET460 3.8 54.0 1.0 C A:GLY203 4.0 28.0 1.0 HD1 A:PHE459 4.1 64.0 1.0 CB A:PHE459 4.1 42.0 1.0 CG A:LYS204 4.2 34.0 1.0 CA A:LYS204 4.2 32.0 1.0 H A:PHE459 4.2 38.0 1.0 SG A:CYS251 4.3 32.0 1.0 C A:LYS204 4.3 28.0 1.0 CA A:MET460 4.3 42.0 1.0 CB A:GLU205 4.4 70.0 1.0 HZ2 A:LYS204 4.4 40.0 1.0 CA A:GLU205 4.5 40.0 1.0 C A:PHE459 4.5 44.0 1.0 CE1 A:PHE252 4.6 54.0 1.0 N A:PHE459 4.6 38.0 1.0 CA A:PHE459 4.6 40.0 1.0 HG A:CYS251 4.6 32.0 1.0 HB2 A:PHE459 4.7 42.0 1.0 OE1 A:GLU205 4.7 50.0 1.0 HD3 A:PRO461 4.7 34.0 1.0 HA A:GLU205 4.7 40.0 1.0 HB3 A:MET460 4.8 54.0 1.0 CB A:LYS204 4.8 54.0 1.0 HA A:MET460 4.8 42.0 1.0 HB2 A:GLU205 4.9 70.0 1.0 HD1 A:PHE252 4.9 48.0 1.0 CD1 A:PHE459 4.9 64.0 1.0 HD2 A:PRO461 4.9 34.0 1.0 CG A:PHE459 5.0 40.0 1.0

Chlorine binding site 2 out of 2 in the Cryo-Em Structure of the Human Clc-2 Chloride Channel Transmembrane Domain with Symmetric C-Terminal


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Cryo-Em Structure of the Human Clc-2 Chloride Channel Transmembrane Domain with Symmetric C-Terminal within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl901 b:32.0 occ:1.00 H B:LYS204 2.3 38.0 1.0 H B:MET460 2.4 48.0 1.0 H B:GLU205 3.0 38.0 1.0 HB3 B:PHE459 3.0 50.0 1.0 HG2 B:MET460 3.0 62.0 1.0 HB2 B:MET460 3.1 36.0 1.0 HG2 B:LYS204 3.1 44.0 1.0 HA3 B:GLY203 3.2 40.0 1.0 HB3 B:GLU205 3.2 104.0 1.0 N B:LYS204 3.3 38.0 1.0 HA2 B:GLY203 3.4 40.0 1.0 N B:MET460 3.4 48.0 1.0 HG3 B:MET460 3.6 62.0 1.0 CG B:MET460 3.6 62.0 1.0 HE1 B:PHE252 3.6 64.0 1.0 CA B:GLY203 3.7 40.0 1.0 CB B:MET460 3.7 36.0 1.0 N B:GLU205 3.8 38.0 1.0 HD1 B:PHE459 3.9 34.0 1.0 C B:GLY203 4.0 30.0 1.0 H B:PHE459 4.0 42.0 1.0 CB B:PHE459 4.0 50.0 1.0 CA B:MET460 4.1 50.0 1.0 CG B:LYS204 4.2 44.0 1.0 CB B:GLU205 4.2 104.0 1.0 CA B:LYS204 4.2 42.0 1.0 C B:PHE459 4.3 44.0 1.0 N B:PHE459 4.3 42.0 1.0 OE1 B:GLU205 4.4 80.0 1.0 C B:LYS204 4.4 34.0 1.0 CA B:PHE459 4.4 32.0 1.0 HD3 B:PRO461 4.4 32.0 1.0 SG B:CYS251 4.5 34.0 1.0 CA B:GLU205 4.5 50.0 1.0 CE1 B:PHE252 4.6 64.0 1.0 HB2 B:PHE459 4.6 50.0 1.0 HA B:MET460 4.7 50.0 1.0 HD3 B:LYS204 4.7 40.0 1.0 HB3 B:MET460 4.7 36.0 1.0 HD2 B:PRO461 4.7 32.0 1.0 CD1 B:PHE459 4.7 34.0 1.0 HG B:CYS251 4.7 34.0 1.0 HG3 B:LYS204 4.7 44.0 1.0 CB B:LYS204 4.8 52.0 1.0 HB2 B:GLU205 4.8 104.0 1.0 HA B:GLU205 4.8 50.0 1.0 CG B:PHE459 4.9 36.0 1.0 CD B:LYS204 5.0 40.0 1.0

M.Xu, T.Neelands, A.S.Powers, Y.Liu, S.Miller, G.Pintilie, J.Du Bois, R.O.Dror, W.Chiu, M.Maduke. Cryo-Em Structures of the Human Clc-2 Voltage Gated Chloride Channel Reveal A Closed Conformational State and Pore Block By An N-Terminal Hairpin Peptide To Be Published.