Potassium in PDB 6wlv: TASK2 in MSP1D1 Lipid Nanodisc at pH 6.5

The binding sites of Potassium atom in the TASK2 in MSP1D1 Lipid Nanodisc at pH 6.5 (pdb code 6wlv). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the TASK2 in MSP1D1 Lipid Nanodisc at pH 6.5, PDB code: 6wlv:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 in the TASK2 in MSP1D1 Lipid Nanodisc at pH 6.5


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of TASK2 in MSP1D1 Lipid Nanodisc at pH 6.5 within 5.0Å range: probe atom residue distance (Å) B Occ A:K401 b:39.9 occ:1.00 O B:ILE204 2.6 34.8 1.0 O A:ILE204 2.6 31.3 1.0 O A:GLY100 2.6 34.8 1.0 O B:GLY100 2.6 34.9 1.0 O B:ILE99 2.7 33.1 1.0 O B:GLY205 2.7 33.9 1.0 K A:K402 2.8 34.2 1.0 O A:GLY205 2.8 33.0 1.0 O A:ILE99 2.8 34.2 1.0 C A:GLY100 3.6 34.8 1.0 C B:GLY205 3.6 33.9 1.0 C B:GLY100 3.6 34.9 1.0 C A:GLY205 3.7 33.0 1.0 C B:ILE204 3.7 34.8 1.0 C A:ILE204 3.8 31.3 1.0 C B:ILE99 3.9 33.1 1.0 C A:ILE99 4.0 34.2 1.0 CA B:GLY205 4.0 33.9 1.0 CA A:GLY100 4.1 34.8 1.0 CA A:GLY205 4.2 33.0 1.0 CA B:GLY100 4.2 34.9 1.0 N B:GLY205 4.4 33.9 1.0 O B:TYR101 4.4 36.0 1.0 N A:GLY205 4.4 33.0 1.0 N B:GLY100 4.5 34.9 1.0 N A:GLY100 4.6 34.8 1.0 N A:TYR101 4.6 37.5 1.0 N B:TYR101 4.6 36.0 1.0 N B:PHE206 4.7 35.6 1.0 N A:PHE206 4.7 34.5 1.0 O A:TYR101 4.8 37.5 1.0 C B:TYR101 4.9 36.0 1.0 CA B:TYR101 4.9 36.0 1.0 CA A:ILE204 4.9 31.3 1.0 CA B:ILE204 4.9 34.8 1.0 C A:TYR101 5.0 37.5 1.0 CA A:TYR101 5.0 37.5 1.0 CA B:ILE99 5.0 33.1 1.0

Potassium binding site 2 out of 3 in the TASK2 in MSP1D1 Lipid Nanodisc at pH 6.5


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of TASK2 in MSP1D1 Lipid Nanodisc at pH 6.5 within 5.0Å range: probe atom residue distance (Å) B Occ A:K402 b:34.2 occ:1.00 O A:ILE99 2.8 34.2 1.0 O B:THR98 2.8 35.4 1.0 K A:K401 2.8 39.9 1.0 O B:THR203 2.8 34.9 1.0 O B:ILE204 2.8 34.8 1.0 O A:THR203 2.8 32.1 1.0 O A:ILE204 2.8 31.3 1.0 O B:ILE99 2.9 33.1 1.0 O A:THR98 2.9 36.5 1.0 C B:ILE204 3.6 34.8 1.0 C A:ILE204 3.6 31.3 1.0 K A:K403 3.6 34.6 1.0 C B:ILE99 3.6 33.1 1.0 C A:ILE99 3.7 34.2 1.0 C A:THR203 3.9 32.1 1.0 C B:THR98 3.9 35.4 1.0 C B:THR203 3.9 34.9 1.0 CA A:ILE204 3.9 31.3 1.0 CA B:ILE204 4.0 34.8 1.0 CA B:ILE99 4.0 33.1 1.0 C A:THR98 4.1 36.5 1.0 CA A:ILE99 4.2 34.2 1.0 N A:ILE204 4.4 31.3 1.0 N B:ILE204 4.4 34.8 1.0 N B:ILE99 4.4 33.1 1.0 N B:GLY205 4.6 33.9 1.0 N A:GLY205 4.6 33.0 1.0 N A:ILE99 4.6 34.2 1.0 N A:GLY100 4.6 34.8 1.0 N B:GLY100 4.7 34.9 1.0 O A:GLY100 4.7 34.8 1.0 O B:GLY100 4.7 34.9 1.0 O B:GLY205 4.9 33.9 1.0 O A:GLY205 4.9 33.0 1.0 CA A:GLY100 4.9 34.8 1.0 CA B:GLY205 4.9 33.9 1.0

Potassium binding site 3 out of 3 in the TASK2 in MSP1D1 Lipid Nanodisc at pH 6.5


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of TASK2 in MSP1D1 Lipid Nanodisc at pH 6.5 within 5.0Å range: probe atom residue distance (Å) B Occ A:K403 b:34.6 occ:1.00 O B:THR98 2.8 35.4 1.0 O A:THR203 2.8 32.1 1.0 OG1 A:THR203 2.9 32.1 1.0 O B:THR203 2.9 34.9 1.0 OG1 B:THR203 2.9 34.9 1.0 O A:THR98 2.9 36.5 1.0 OG1 A:THR98 2.9 36.5 1.0 OG1 B:THR98 3.0 35.4 1.0 CB B:THR98 3.4 35.4 1.0 CB A:THR98 3.5 36.5 1.0 CB A:THR203 3.5 32.1 1.0 K A:K402 3.6 34.2 1.0 CB B:THR203 3.6 34.9 1.0 C B:THR98 3.8 35.4 1.0 C B:THR203 3.9 34.9 1.0 C A:THR203 3.9 32.1 1.0 C A:THR98 3.9 36.5 1.0 CA B:THR98 4.3 35.4 1.0 CA A:THR98 4.3 36.5 1.0 CA A:THR203 4.3 32.1 1.0 CA B:THR203 4.4 34.9 1.0 CG2 B:THR98 4.6 35.4 1.0 O B:SER202 4.7 34.5 1.0 CG2 A:THR98 4.7 36.5 1.0 CG2 A:THR203 4.7 32.1 1.0 CG2 B:THR203 4.9 34.9 1.0 N B:ILE204 4.9 34.8 1.0 N B:ILE99 4.9 33.1 1.0 N A:ILE99 4.9 34.2 1.0 O A:SER202 5.0 34.9 1.0 N A:ILE204 5.0 31.3 1.0

B.Li, R.A.Rietmeijer, S.G.Brohawn. Structural Basis For pH Gating of the Two-Pore Domain K + Channel TASK2. Nature V. 586 457 2020.
ISSN: ESSN 1476-4687
PubMed: 32999458
DOI: 10.1038/S41586-020-2770-2