Chlorine in PDB 8tnw: Substrate Binding Plasticity Revealed By Cryo-Em Structures of SLC26A2

The binding sites of Chlorine atom in the Substrate Binding Plasticity Revealed By Cryo-Em Structures of SLC26A2 (pdb code 8tnw). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Substrate Binding Plasticity Revealed By Cryo-Em Structures of SLC26A2, PDB code: 8tnw:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Substrate Binding Plasticity Revealed By Cryo-Em Structures of SLC26A2


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Substrate Binding Plasticity Revealed By Cryo-Em Structures of SLC26A2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl801 b:20.0 occ:1.00 N A:GLY166 3.2 47.6 1.0 CE1 A:PHE165 3.3 54.6 1.0 CD1 A:PHE165 3.4 55.8 1.0 CA A:GLY166 3.6 43.9 1.0 OH A:TYR129 4.0 73.1 1.0 N A:VAL167 4.3 40.6 1.0 C A:PHE165 4.3 54.3 1.0 C A:GLY166 4.5 47.8 1.0 CZ A:PHE165 4.5 51.6 1.0 CG A:PHE165 4.5 52.8 1.0 CZ A:TYR129 4.6 75.1 1.0 CA A:PHE165 4.6 49.8 1.0 CE2 A:TYR129 4.8 70.2 1.0 CD2 A:LEU491 4.9 47.8 1.0

Chlorine binding site 2 out of 2 in the Substrate Binding Plasticity Revealed By Cryo-Em Structures of SLC26A2


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Substrate Binding Plasticity Revealed By Cryo-Em Structures of SLC26A2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl801 b:20.0 occ:1.00 N B:GLY166 3.2 47.6 1.0 CE1 B:PHE165 3.3 54.6 1.0 CD1 B:PHE165 3.4 55.8 1.0 CA B:GLY166 3.6 43.9 1.0 OH B:TYR129 4.0 73.1 1.0 N B:VAL167 4.3 40.6 1.0 C B:PHE165 4.3 54.3 1.0 C B:GLY166 4.5 47.8 1.0 CZ B:PHE165 4.5 51.6 1.0 CG B:PHE165 4.5 52.8 1.0 CZ B:TYR129 4.6 75.1 1.0 CA B:PHE165 4.6 49.8 1.0 CE2 B:TYR129 4.8 70.2 1.0 CD2 B:LEU491 4.9 47.8 1.0

W.Hu, A.Song, H.Zheng. Substrate Binding Plasticity Revealed By Cryo-Em Structures of SLC26A2. Nat Commun V. 15 3616 2024.
ISSN: ESSN 2041-1723
PubMed: 38684689
DOI: 10.1038/S41467-024-48028-3