Zinc in PDB 7x6c: Cryo-Em Structure of the Human TRPC5 Ion Channel in Lipid Nanodiscs, CLASS1

The structure of Cryo-Em Structure of the Human TRPC5 Ion Channel in Lipid Nanodiscs, CLASS1 also contains other interesting chemical elements:

Calcium

(Ca)

4 atoms

The binding sites of Zinc atom in the Cryo-Em Structure of the Human TRPC5 Ion Channel in Lipid Nanodiscs, CLASS1 (pdb code 7x6c). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Cryo-Em Structure of the Human TRPC5 Ion Channel in Lipid Nanodiscs, CLASS1, PDB code: 7x6c:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Cryo-Em Structure of the Human TRPC5 Ion Channel in Lipid Nanodiscs, CLASS1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cryo-Em Structure of the Human TRPC5 Ion Channel in Lipid Nanodiscs, CLASS1 within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn804 b:129.4 occ:1.00 ND1 C:HIS172 2.1 60.0 1.0 SG C:CYS181 2.3 63.4 1.0 SG C:CYS178 2.3 73.1 1.0 SG C:CYS176 2.3 72.2 1.0 CE1 C:HIS172 2.8 60.0 1.0 CB C:CYS176 2.9 72.2 1.0 CG C:HIS172 3.0 60.0 1.0 CB C:CYS181 3.3 63.4 1.0 CB C:HIS172 3.5 60.0 1.0 NE2 C:HIS172 3.8 60.0 1.0 CD2 C:HIS172 3.9 60.0 1.0 CB C:CYS178 4.1 73.1 1.0 CA C:CYS176 4.3 72.2 1.0 N C:CYS181 4.5 63.4 1.0 CA C:CYS181 4.5 63.4 1.0 CA C:HIS172 4.9 60.0 1.0 N C:CYS178 4.9 73.1 1.0

Zinc binding site 2 out of 4 in the Cryo-Em Structure of the Human TRPC5 Ion Channel in Lipid Nanodiscs, CLASS1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Cryo-Em Structure of the Human TRPC5 Ion Channel in Lipid Nanodiscs, CLASS1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn804 b:126.2 occ:1.00 ND1 A:HIS172 2.1 60.6 1.0 SG A:CYS181 2.3 63.4 1.0 SG A:CYS178 2.3 72.8 1.0 SG A:CYS176 2.3 72.0 1.0 CE1 A:HIS172 2.8 60.6 1.0 CB A:CYS176 2.9 72.0 1.0 CG A:HIS172 3.0 60.6 1.0 CB A:CYS181 3.3 63.4 1.0 CB A:HIS172 3.5 60.6 1.0 NE2 A:HIS172 3.8 60.6 1.0 CD2 A:HIS172 3.9 60.6 1.0 CB A:CYS178 4.1 72.8 1.0 CA A:CYS176 4.3 72.0 1.0 N A:CYS181 4.5 63.4 1.0 CA A:CYS181 4.5 63.4 1.0 CA A:HIS172 4.9 60.6 1.0 N A:CYS178 4.9 72.8 1.0

Zinc binding site 3 out of 4 in the Cryo-Em Structure of the Human TRPC5 Ion Channel in Lipid Nanodiscs, CLASS1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Cryo-Em Structure of the Human TRPC5 Ion Channel in Lipid Nanodiscs, CLASS1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn805 b:119.7 occ:1.00 ND1 B:HIS172 2.1 58.8 1.0 SG B:CYS181 2.3 62.0 1.0 SG B:CYS178 2.3 72.8 1.0 SG B:CYS176 2.3 71.8 1.0 CE1 B:HIS172 2.8 58.8 1.0 CB B:CYS176 2.9 71.8 1.0 CG B:HIS172 3.0 58.8 1.0 CB B:CYS181 3.3 62.0 1.0 CB B:HIS172 3.5 58.8 1.0 NE2 B:HIS172 3.8 58.8 1.0 CD2 B:HIS172 3.9 58.8 1.0 CB B:CYS178 4.1 72.8 1.0 CA B:CYS176 4.3 71.8 1.0 N B:CYS181 4.5 62.0 1.0 CA B:CYS181 4.5 62.0 1.0 CA B:HIS172 4.9 58.8 1.0 N B:CYS178 4.9 72.8 1.0

Zinc binding site 4 out of 4 in the Cryo-Em Structure of the Human TRPC5 Ion Channel in Lipid Nanodiscs, CLASS1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Cryo-Em Structure of the Human TRPC5 Ion Channel in Lipid Nanodiscs, CLASS1 within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn805 b:119.4 occ:1.00 ND1 D:HIS172 2.1 59.0 1.0 SG D:CYS181 2.3 62.0 1.0 SG D:CYS178 2.3 72.2 1.0 SG D:CYS176 2.3 71.4 1.0 CE1 D:HIS172 2.8 59.0 1.0 CB D:CYS176 2.9 71.4 1.0 CG D:HIS172 3.0 59.0 1.0 CB D:CYS181 3.3 62.0 1.0 CB D:HIS172 3.5 59.0 1.0 NE2 D:HIS172 3.8 59.0 1.0 CD2 D:HIS172 3.9 59.0 1.0 CB D:CYS178 4.1 72.2 1.0 CA D:CYS176 4.3 71.4 1.0 N D:CYS181 4.5 62.0 1.0 CA D:CYS181 4.5 62.0 1.0 CA D:HIS172 4.9 59.0 1.0 N D:CYS178 4.9 72.2 1.0

J.Won, J.Kim, H.Jeong, J.Kim, S.Feng, B.Jeong, M.Kwak, J.Ko, W.Im, I.So, H.H.Lee. Molecular Architecture of the G Alpha I -Bound TRPC5 Ion Channel. Nat Commun V. 14 2550 2023.
ISSN: ESSN 2041-1723
PubMed: 37137991
DOI: 10.1038/S41467-023-38281-3