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Potassium in PDB 7mxo: Cryo-Em Structure of Human NKCC1

Other elements in 7mxo:

The structure of Cryo-Em Structure of Human NKCC1 also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Cryo-Em Structure of Human NKCC1 (pdb code 7mxo). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Cryo-Em Structure of Human NKCC1, PDB code: 7mxo:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 7mxo

Go back to Potassium Binding Sites List in 7mxo
Potassium binding site 1 out of 2 in the Cryo-Em Structure of Human NKCC1


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 Human NKCC1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1302

b:40.0
occ:1.00
O A:PRO496 2.6 44.3 1.0
OH A:TYR383 2.7 50.2 1.0
O A:THR499 2.8 44.0 1.0
CL A:CL1301 3.0 51.8 1.0
O A:ILE299 3.3 43.9 1.0
O A:ASN298 3.6 48.5 1.0
C A:PRO496 3.8 44.3 1.0
CZ A:TYR383 3.8 50.2 1.0
C A:THR499 4.0 44.0 1.0
OG1 A:THR499 4.1 44.0 1.0
C A:ILE299 4.1 43.9 1.0
CE1 A:TYR383 4.2 50.2 1.0
C A:ALA497 4.2 44.3 1.0
CA A:ALA497 4.3 44.3 1.0
O A:ALA497 4.3 44.3 1.0
N A:THR499 4.3 44.0 1.0
CA A:ILE299 4.4 43.9 1.0
N A:ALA497 4.5 44.3 1.0
N A:GLY301 4.6 46.3 1.0
CA A:THR499 4.6 44.0 1.0
CA A:GLY301 4.7 46.3 1.0
C A:ASN298 4.7 48.5 1.0
N A:ALA498 4.8 42.1 1.0
CA A:PRO496 4.8 44.3 1.0
OD1 A:ASN298 4.9 48.5 1.0
CE2 A:TYR383 5.0 50.2 1.0
CB A:THR499 5.0 44.0 1.0

Potassium binding site 2 out of 2 in 7mxo

Go back to Potassium Binding Sites List in 7mxo
Potassium binding site 2 out of 2 in the Cryo-Em Structure of Human NKCC1


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 Human NKCC1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K1302

b:42.8
occ:1.00
OH B:TYR383 2.7 36.3 1.0
O B:PRO496 2.7 33.5 1.0
CL B:CL1301 2.8 31.2 1.0
O B:THR499 2.8 34.3 1.0
O B:ILE299 2.9 32.4 1.0
O B:ASN298 3.2 38.1 1.0
C B:ILE299 3.7 32.4 1.0
CZ B:TYR383 3.8 36.3 1.0
C B:PRO496 4.0 33.5 1.0
CA B:ILE299 4.0 32.4 1.0
C B:THR499 4.0 34.3 1.0
OG1 B:THR499 4.1 34.3 1.0
CE1 B:TYR383 4.2 36.3 1.0
C B:ASN298 4.3 38.1 1.0
N B:THR499 4.4 34.3 1.0
C B:ALA497 4.4 32.3 1.0
O B:ALA497 4.5 32.3 1.0
N B:GLY301 4.6 34.5 1.0
CA B:ALA497 4.6 32.3 1.0
N B:ILE299 4.6 32.4 1.0
CA B:THR499 4.7 34.3 1.0
CA B:GLY301 4.7 34.5 1.0
N B:ALA497 4.8 32.3 1.0
N B:ALA498 4.8 31.0 1.0
N B:TRP300 4.9 32.0 1.0
OD1 B:ASN298 4.9 38.1 1.0
CE2 B:TYR383 4.9 36.3 1.0
CA B:PRO496 4.9 33.5 1.0

Reference:

M.A.Moseng, C.C.Su, K.Rios, M.Cui, M.Lyu, P.Glaza, P.A.Klenotic, E.Delpire, E.W.Yu. Inhibition Mechanism of NKCC1 Involves the Carboxyl Terminus and Long-Range Conformational Coupling. Sci Adv V. 8 Q0952 2022.
ISSN: ESSN 2375-2548
PubMed: 36306358
DOI: 10.1126/SCIADV.ABQ0952
Page generated: Mon Aug 12 19:28:13 2024

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