Potassium in PDB 7wsw: Cryo-Em Structure of the Potassium Channel AKT1 From Arabidopsis Thaliana

The binding sites of Potassium atom in the Cryo-Em Structure of the Potassium Channel AKT1 From Arabidopsis Thaliana (pdb code 7wsw). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the Cryo-Em Structure of the Potassium Channel AKT1 From Arabidopsis Thaliana, PDB code: 7wsw:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 in the Cryo-Em Structure of the Potassium Channel AKT1 From Arabidopsis Thaliana


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Cryo-Em Structure of the Potassium Channel AKT1 From Arabidopsis Thaliana within 5.0Å range: probe atom residue distance (Å) B Occ A:K902 b:58.4 occ:1.00 O A:THR253 2.8 51.2 1.0 O D:VAL254 2.8 51.7 1.0 O B:VAL254 2.8 52.2 1.0 O A:VAL254 2.8 50.4 1.0 O C:VAL254 2.8 50.5 1.0 O C:THR253 2.9 51.0 1.0 O D:THR253 2.9 52.1 1.0 O B:THR253 2.9 52.5 1.0 C B:VAL254 3.6 52.2 1.0 C D:VAL254 3.6 51.7 1.0 K A:K903 3.6 48.9 1.0 C C:VAL254 3.6 50.5 1.0 C A:VAL254 3.6 50.4 1.0 C A:THR253 3.9 51.2 1.0 C D:THR253 3.9 52.1 1.0 C B:THR253 3.9 52.5 1.0 C C:THR253 3.9 51.0 1.0 CA D:VAL254 4.0 51.7 1.0 CA B:VAL254 4.0 52.2 1.0 CA A:VAL254 4.0 50.4 1.0 CA C:VAL254 4.0 50.5 1.0 N D:VAL254 4.4 51.7 1.0 N B:VAL254 4.4 52.2 1.0 N A:VAL254 4.4 50.4 1.0 N C:VAL254 4.4 50.5 1.0 N B:GLY255 4.6 54.7 1.0 N C:GLY255 4.6 54.2 1.0 N D:GLY255 4.6 54.2 1.0 N A:GLY255 4.6 54.1 1.0

Potassium binding site 2 out of 3 in the Cryo-Em Structure of the Potassium Channel AKT1 From Arabidopsis Thaliana


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Cryo-Em Structure of the Potassium Channel AKT1 From Arabidopsis Thaliana within 5.0Å range: probe atom residue distance (Å) B Occ A:K903 b:48.9 occ:1.00 OG1 A:THR253 2.8 51.2 1.0 OG1 C:THR253 2.8 51.0 1.0 OG1 D:THR253 2.8 52.1 1.0 OG1 B:THR253 2.8 52.5 1.0 O B:THR253 2.8 52.5 1.0 O D:THR253 2.8 52.1 1.0 O C:THR253 2.9 51.0 1.0 O A:THR253 2.9 51.2 1.0 CB A:THR253 3.6 51.2 1.0 CB D:THR253 3.6 52.1 1.0 CB C:THR253 3.6 51.0 1.0 CB B:THR253 3.6 52.5 1.0 K A:K902 3.6 58.4 1.0 C B:THR253 3.9 52.5 1.0 C D:THR253 3.9 52.1 1.0 C C:THR253 3.9 51.0 1.0 C A:THR253 3.9 51.2 1.0 CA D:THR253 4.4 52.1 1.0 CA B:THR253 4.4 52.5 1.0 CA A:THR253 4.4 51.2 1.0 CA C:THR253 4.4 51.0 1.0 O C:THR252 4.8 50.3 1.0 O A:THR252 4.8 50.4 1.0 CG2 A:THR253 4.8 51.2 1.0 CG2 C:THR253 4.8 51.0 1.0 CG2 D:THR253 4.8 52.1 1.0 CG2 B:THR253 4.8 52.5 1.0 O B:THR252 4.8 51.8 1.0 O D:THR252 4.8 51.3 1.0

Potassium binding site 3 out of 3 in the Cryo-Em Structure of the Potassium Channel AKT1 From Arabidopsis Thaliana


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Cryo-Em Structure of the Potassium Channel AKT1 From Arabidopsis Thaliana within 5.0Å range: probe atom residue distance (Å) B Occ A:K904 b:74.4 occ:1.00 O D:GLY255 2.8 54.2 1.0 O B:GLY255 2.8 54.7 1.0 O C:TYR256 2.8 56.1 1.0 O A:TYR256 2.8 56.1 1.0 O C:GLY255 2.9 54.2 1.0 O A:GLY255 2.9 54.1 1.0 O D:TYR256 2.9 56.1 1.0 O B:TYR256 2.9 56.4 1.0 C D:TYR256 3.5 56.1 1.0 C B:TYR256 3.5 56.4 1.0 C C:TYR256 3.6 56.1 1.0 C A:TYR256 3.6 56.1 1.0 C D:GLY255 4.0 54.2 1.0 C B:GLY255 4.0 54.7 1.0 C C:GLY255 4.0 54.2 1.0 C A:GLY255 4.0 54.1 1.0 CA D:TYR256 4.2 56.1 1.0 CA B:TYR256 4.2 56.4 1.0 CA A:TYR256 4.2 56.1 1.0 CA C:TYR256 4.2 56.1 1.0 N B:GLY257 4.2 61.2 1.0 N D:GLY257 4.2 60.4 1.0 N C:GLY257 4.4 60.6 1.0 N A:GLY257 4.4 61.3 1.0 CA B:GLY257 4.4 61.2 1.0 CA D:GLY257 4.4 60.4 1.0 CA C:GLY257 4.6 60.6 1.0 CA A:GLY257 4.6 61.3 1.0 N D:TYR256 4.6 56.1 1.0 N B:TYR256 4.6 56.4 1.0 N C:TYR256 4.6 56.1 1.0 N A:TYR256 4.6 56.1 1.0

Y.Lu, M.Yu, Y.Jia, F.Yang, Y.Zhang, X.Xu, X.Li, F.Yang, J.Lei, Y.Wang, G.Yang. Structural Basis For the Activity Regulation of A Potassium Channel AKT1 From Arabidopsis. Nat Commun V. 13 5682 2022.
ISSN: ESSN 2041-1723
PubMed: 36167696
DOI: 10.1038/S41467-022-33420-8