Zinc in PDB 8hkq: Ion Channel

The structure of Ion Channel also contains other interesting chemical elements:

Fluorine	(F)	12 atoms
Sodium	(Na)	1 atom
Potassium	(K)	11 atoms

The binding sites of Zinc atom in the Ion Channel (pdb code 8hkq). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Ion Channel, PDB code: 8hkq:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Ion Channel


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Ion Channel within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn1302 b:169.7 occ:1.00 ND1 D:HIS787 2.1 125.7 1.0 SG D:CYS785 2.3 124.1 1.0 SG D:CYS777 2.3 73.4 1.0 SG D:CYS778 2.3 80.2 1.0 CE1 D:HIS787 2.8 123.9 1.0 CB D:CYS785 3.1 119.0 1.0 CG D:HIS787 3.2 124.0 1.0 N D:CYS778 3.5 69.2 1.0 CB D:CYS778 3.6 72.0 1.0 CB D:HIS787 3.7 123.7 1.0 CA D:CYS778 3.7 70.3 1.0 CB D:CYS777 3.8 71.3 1.0 N D:HIS787 3.9 124.4 1.0 C D:CYS777 3.9 70.7 1.0 NE2 D:HIS787 4.0 123.6 1.0 CD2 D:HIS787 4.2 124.0 1.0 CA D:HIS787 4.4 124.3 1.0 CG D:PRO775 4.4 59.3 1.0 N D:LYS786 4.4 124.1 1.0 O D:CYS777 4.4 72.8 1.0 CA D:CYS785 4.4 119.6 1.0 CA D:CYS777 4.4 70.5 1.0 N D:ASN788 4.6 124.5 1.0 C D:CYS785 4.7 120.2 1.0 C D:HIS787 4.9 125.0 1.0

Zinc binding site 2 out of 4 in the Ion Channel


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Ion Channel within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1302 b:182.1 occ:1.00 ND1 A:HIS787 2.1 126.6 1.0 SG A:CYS785 2.3 120.4 1.0 SG A:CYS777 2.3 76.3 1.0 SG A:CYS778 2.3 80.2 1.0 CE1 A:HIS787 2.8 124.4 1.0 CB A:CYS785 3.1 116.7 1.0 CG A:HIS787 3.2 125.2 1.0 N A:CYS778 3.5 71.2 1.0 CB A:CYS778 3.6 72.5 1.0 CB A:HIS787 3.7 124.8 1.0 CA A:CYS778 3.7 71.8 1.0 CB A:CYS777 3.8 73.7 1.0 N A:HIS787 3.9 125.0 1.0 C A:CYS777 3.9 73.2 1.0 NE2 A:HIS787 4.0 124.0 1.0 CD2 A:HIS787 4.2 124.6 1.0 CA A:HIS787 4.3 124.7 1.0 CG A:PRO775 4.4 57.1 1.0 N A:LYS786 4.4 121.2 1.0 O A:CYS777 4.4 74.4 1.0 CA A:CYS785 4.4 117.1 1.0 CA A:CYS777 4.4 72.5 1.0 N A:ASN788 4.6 121.7 1.0 C A:CYS785 4.7 118.0 1.0 C A:HIS787 4.9 125.2 1.0

Zinc binding site 3 out of 4 in the Ion Channel


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Ion Channel within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn1302 b:174.9 occ:1.00 ND1 C:HIS787 2.1 127.3 1.0 SG C:CYS785 2.3 123.2 1.0 SG C:CYS777 2.3 76.4 1.0 SG C:CYS778 2.3 82.1 1.0 CE1 C:HIS787 2.8 125.2 1.0 CB C:CYS785 3.1 119.0 1.0 CG C:HIS787 3.2 125.4 1.0 N C:CYS778 3.5 71.3 1.0 CB C:CYS778 3.6 73.5 1.0 CB C:HIS787 3.7 125.2 1.0 CA C:CYS778 3.7 71.9 1.0 CB C:CYS777 3.8 74.0 1.0 N C:HIS787 3.9 125.6 1.0 C C:CYS777 3.9 72.9 1.0 NE2 C:HIS787 4.0 124.8 1.0 CD2 C:HIS787 4.2 124.9 1.0 CA C:HIS787 4.4 125.3 1.0 N C:LYS786 4.4 124.5 1.0 CG C:PRO775 4.4 59.3 1.0 O C:CYS777 4.4 74.8 1.0 CA C:CYS785 4.4 119.6 1.0 CA C:CYS777 4.4 73.1 1.0 N C:ASN788 4.6 123.8 1.0 C C:CYS785 4.7 120.6 1.0 C C:HIS787 4.9 125.8 1.0

Zinc binding site 4 out of 4 in the Ion Channel


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Ion Channel within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1302 b:173.8 occ:1.00 ND1 B:HIS787 2.1 125.4 1.0 SG B:CYS785 2.3 122.2 1.0 SG B:CYS778 2.3 80.5 1.0 SG B:CYS777 2.3 74.8 1.0 CE1 B:HIS787 2.8 123.3 1.0 CB B:CYS785 3.1 117.5 1.0 CG B:HIS787 3.2 123.8 1.0 N B:CYS778 3.5 69.9 1.0 CB B:CYS778 3.6 72.1 1.0 CB B:HIS787 3.7 123.2 1.0 CA B:CYS778 3.7 69.9 1.0 CB B:CYS777 3.8 72.5 1.0 C B:CYS777 3.9 71.3 1.0 N B:HIS787 3.9 123.2 1.0 NE2 B:HIS787 4.0 122.6 1.0 CD2 B:HIS787 4.2 123.3 1.0 CG B:PRO775 4.3 55.6 1.0 CA B:HIS787 4.4 123.1 1.0 N B:LYS786 4.4 122.3 1.0 O B:CYS777 4.4 73.4 1.0 CA B:CYS785 4.4 118.0 1.0 CA B:CYS777 4.4 70.8 1.0 N B:ASN788 4.6 123.9 1.0 C B:CYS785 4.7 119.1 1.0 C B:HIS787 4.9 123.9 1.0

J.Zhang, S.Liu, J.Fan, R.Yan, B.Huang, F.Zhou, T.Yuan, J.Gong, Z.Huang, D.Jiang. Structural Basis of Human SLO2.2 Channel Gating and Modulation. Cell Rep V. 42 12858 2023.
ISSN: ESSN 2211-1247
PubMed: 37494189
DOI: 10.1016/J.CELREP.2023.112858