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Potassium in PDB 7xuf: Cryo-Em Structure of the AKT1-ATKC1 Complex From Arabidopsis Thaliana

Potassium Binding Sites:

The binding sites of Potassium atom in the Cryo-Em Structure of the AKT1-ATKC1 Complex From Arabidopsis Thaliana (pdb code 7xuf). 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 AKT1-ATKC1 Complex From Arabidopsis Thaliana, PDB code: 7xuf:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 in 7xuf

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Potassium binding site 1 out of 3 in the Cryo-Em Structure of the AKT1-ATKC1 Complex 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 AKT1-ATKC1 Complex From Arabidopsis Thaliana within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K701

b:50.2
occ:1.00
O A:THR289 3.1 50.2 1.0
O D:THR253 3.2 7.4 1.0
K A:K702 3.2 19.0 1.0
O C:THR289 3.3 10.6 1.0
O B:THR253 3.4 50.2 1.0
N A:GLY291 3.8 4.8 1.0
N D:GLY255 3.8 50.2 1.0
N B:GLY255 3.9 12.3 1.0
N C:GLY291 4.0 7.8 1.0
C A:THR289 4.2 50.2 1.0
CA A:VAL290 4.2 3.3 1.0
C D:THR253 4.3 7.4 1.0
CA B:VAL254 4.3 6.3 1.0
CA D:VAL254 4.4 17.4 1.0
C B:THR253 4.4 50.2 1.0
CA C:VAL290 4.4 50.2 1.0
C C:THR289 4.4 10.6 1.0
C A:VAL290 4.4 3.3 1.0
C D:VAL254 4.6 17.4 1.0
C C:VAL290 4.6 50.2 1.0
C B:VAL254 4.6 6.3 1.0
N A:VAL290 4.7 3.3 1.0
CA A:GLY291 4.7 4.8 1.0
CA D:GLY255 4.8 50.2 1.0
N D:VAL254 4.8 17.4 1.0
N B:VAL254 4.8 6.3 1.0
O D:GLY255 4.9 50.2 1.0
CA B:GLY255 4.9 12.3 1.0
N C:VAL290 4.9 50.2 1.0
CA C:GLY291 5.0 7.8 1.0
O A:GLY291 5.0 4.8 1.0

Potassium binding site 2 out of 3 in 7xuf

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Potassium binding site 2 out of 3 in the Cryo-Em Structure of the AKT1-ATKC1 Complex 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 AKT1-ATKC1 Complex From Arabidopsis Thaliana within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K702

b:19.0
occ:1.00
O C:THR289 2.8 10.6 1.0
O A:THR289 2.8 50.2 1.0
O B:THR253 2.9 50.2 1.0
O D:THR253 2.9 7.4 1.0
K A:K701 3.2 50.2 1.0
OG1 A:THR289 3.5 50.2 1.0
OG1 C:THR289 3.6 10.6 1.0
OG1 D:THR253 3.7 7.4 1.0
CB A:THR289 3.7 50.2 1.0
CB C:THR289 3.9 10.6 1.0
C A:THR289 3.9 50.2 1.0
OG1 B:THR253 3.9 50.2 1.0
C C:THR289 3.9 10.6 1.0
CB D:THR253 4.0 7.4 1.0
C D:THR253 4.1 7.4 1.0
C B:THR253 4.1 50.2 1.0
CB B:THR253 4.1 50.2 1.0
CA A:THR289 4.4 50.2 1.0
CA C:THR289 4.5 10.6 1.0
CA D:THR253 4.7 7.4 1.0
CA B:THR253 4.7 50.2 1.0
N A:VAL290 4.9 3.3 1.0
N C:VAL290 4.9 50.2 1.0
CG2 A:THR289 4.9 50.2 1.0

Potassium binding site 3 out of 3 in 7xuf

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Potassium binding site 3 out of 3 in the Cryo-Em Structure of the AKT1-ATKC1 Complex 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 AKT1-ATKC1 Complex From Arabidopsis Thaliana within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K901

b:15.6
occ:1.00
O A:GLY291 2.8 4.8 1.0
O B:GLY255 2.8 12.3 1.0
O D:TYR256 2.8 22.6 1.0
O C:GLY291 2.9 7.8 1.0
O B:TYR256 3.0 21.8 1.0
O D:GLY255 3.0 50.2 1.0
C B:TYR256 3.6 21.8 1.0
C D:TYR256 3.7 22.6 1.0
C A:GLY291 3.9 4.8 1.0
C C:GLY291 3.9 7.8 1.0
C B:GLY255 4.0 12.3 1.0
CA A:TYR292 4.1 10.3 1.0
C D:GLY255 4.1 50.2 1.0
CA C:TYR292 4.2 13.9 1.0
C A:TYR292 4.2 10.3 1.0
N A:GLY293 4.2 46.7 1.0
CA B:TYR256 4.3 21.8 1.0
C C:TYR292 4.3 13.9 1.0
N B:GLY257 4.3 50.2 1.0
CA D:TYR256 4.4 22.6 1.0
CA B:GLY257 4.4 50.2 1.0
N C:GLY293 4.4 29.5 1.0
N D:GLY257 4.4 23.1 1.0
N A:TYR292 4.5 10.3 1.0
CA D:GLY257 4.5 23.1 1.0
N C:TYR292 4.6 13.9 1.0
N B:TYR256 4.6 21.8 1.0
N D:TYR256 4.7 22.6 1.0
O C:TYR292 4.8 13.9 1.0
O A:TYR292 4.8 10.3 1.0

Reference:

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
Page generated: Sat Aug 9 15:16:06 2025

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