Chlorine in PDB 9jcz: Cryo-Em Structure of Human Taut in Presence of Taurine, Determined in An Inward-Facing Occluded Conformation

The structure of Cryo-Em Structure of Human Taut in Presence of Taurine, Determined in An Inward-Facing Occluded Conformation also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Chlorine atom in the Cryo-Em Structure of Human Taut in Presence of Taurine, Determined in An Inward-Facing Occluded Conformation (pdb code 9jcz). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Cryo-Em Structure of Human Taut in Presence of Taurine, Determined in An Inward-Facing Occluded Conformation, PDB code: 9jcz:

Chlorine binding site 1 out of 1 in the Cryo-Em Structure of Human Taut in Presence of Taurine, Determined in An Inward-Facing Occluded Conformation


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 Human Taut in Presence of Taurine, Determined in An Inward-Facing Occluded Conformation within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl705 b:50.3 occ:1.00 OG A:SER337 2.4 44.5 1.0 OG A:SER301 2.9 43.6 0.5 NE2 A:GLN297 3.1 44.1 1.0 OH A:TYR83 3.1 42.4 1.0 CB A:SER337 3.2 44.5 1.0 CB A:SER301 3.2 43.6 0.5 CB A:SER301 3.3 43.6 0.5 OG A:SER301 3.3 43.6 0.5 CG A:GLN297 3.7 44.1 1.0 CD A:GLN297 3.9 44.1 1.0 CZ A:TYR83 4.1 42.4 1.0 CD1 A:PHE67 4.2 39.6 1.0 CE1 A:TYR83 4.3 42.4 1.0 O A:GLN297 4.3 44.1 1.0 O A:GLY62 4.4 38.0 1.0 ND2 A:ASN63 4.5 40.7 1.0 CA A:SER337 4.6 44.5 1.0 CA A:SER301 4.8 43.6 0.5 CA A:SER301 4.8 43.6 0.5 CG A:PHE67 4.8 39.6 1.0 CE1 A:PHE67 4.8 39.6 1.0 CB A:PHE67 4.8 39.6 1.0 CG A:ASN63 4.9 40.7 1.0 C A:GLN297 5.0 44.1 1.0 CB A:GLN297 5.0 44.1 1.0 CA A:ASN63 5.0 40.7 1.0

Y.Chao, Z.Zhou, H.Xia, C.Yang, T.Li, Y.Q.Tang, Y.Shu, Q.Ba, J.Hong, D.Li, Q.Qu. Transport and Inhibition Mechanism For Human Taut-Mediated Taurine Uptake. Cell Res. 2025.
ISSN: ISSN 1001-0602
PubMed: 39837997
DOI: 10.1038/S41422-025-01076-W