Potassium in PDB 7adi: KIRBAC3.1 W46R: Role of A Highly Conserved Tryptophan at the Membrane- Water Interface of Kir Channel

The structure of KIRBAC3.1 W46R: Role of A Highly Conserved Tryptophan at the Membrane- Water Interface of Kir Channel, PDB code: 7adi was solved by C.Venien-Bryan, C.Fagnen, R.De Zorzi, L.Bannwarth, I.Oubella, A.Haouz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.02 / 2.80
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	106.77, 113.98, 89.18, 90, 90, 90
R / Rfree (%)	22.2 / 28.7

The structure of KIRBAC3.1 W46R: Role of A Highly Conserved Tryptophan at the Membrane- Water Interface of Kir Channel also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Potassium atom in the KIRBAC3.1 W46R: Role of A Highly Conserved Tryptophan at the Membrane- Water Interface of Kir Channel (pdb code 7adi). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the KIRBAC3.1 W46R: Role of A Highly Conserved Tryptophan at the Membrane- Water Interface of Kir Channel, PDB code: 7adi:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 in the KIRBAC3.1 W46R: Role of A Highly Conserved Tryptophan at the Membrane- Water Interface of Kir Channel


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of KIRBAC3.1 W46R: Role of A Highly Conserved Tryptophan at the Membrane- Water Interface of Kir Channel within 5.0Å range: probe atom residue distance (Å) B Occ A:K1001 b:111.0 occ:0.25 K A:K1003 2.7 106.9 0.2 O A:TYR99 3.4 174.7 1.0 O B:TYR99 3.6 172.1 1.0 CA A:GLY100 3.9 165.5 1.0 C A:TYR99 4.0 157.4 1.0 C B:TYR99 4.0 155.6 1.0 O A:GLY98 4.1 157.3 1.0 CA B:GLY100 4.1 169.1 1.0 N A:GLY100 4.2 173.8 1.0 O B:GLY98 4.2 168.1 1.0 N B:GLY100 4.3 170.1 1.0 O A:GLY100 4.9 120.6 1.0 C A:GLY100 4.9 151.2 1.0 CA B:TYR99 5.0 130.4 1.0

Potassium binding site 2 out of 3 in the KIRBAC3.1 W46R: Role of A Highly Conserved Tryptophan at the Membrane- Water Interface of Kir Channel


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of KIRBAC3.1 W46R: Role of A Highly Conserved Tryptophan at the Membrane- Water Interface of Kir Channel within 5.0Å range: probe atom residue distance (Å) B Occ A:K1002 b:78.0 occ:0.25 O A:ILE97 2.9 131.0 1.0 O B:ILE97 3.1 119.6 1.0 O A:THR96 3.2 91.3 1.0 O B:THR96 3.3 94.8 1.0 C B:ILE97 3.7 119.2 1.0 C A:ILE97 3.8 142.0 1.0 K A:K1003 3.9 106.9 0.2 MG A:MG1004 3.9 37.2 0.2 C A:THR96 4.2 111.7 1.0 C B:THR96 4.2 96.4 1.0 CA A:ILE97 4.3 134.1 1.0 CA B:ILE97 4.3 108.7 1.0 N B:GLY98 4.5 136.2 1.0 N A:ILE97 4.7 125.5 1.0 N B:ILE97 4.7 95.0 1.0 N A:GLY98 4.7 150.2 1.0 CA B:GLY98 4.8 149.7 1.0

Potassium binding site 3 out of 3 in the KIRBAC3.1 W46R: Role of A Highly Conserved Tryptophan at the Membrane- Water Interface of Kir Channel


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of KIRBAC3.1 W46R: Role of A Highly Conserved Tryptophan at the Membrane- Water Interface of Kir Channel within 5.0Å range: probe atom residue distance (Å) B Occ A:K1003 b:106.9 occ:0.25 K A:K1001 2.7 111.0 0.2 O A:GLY98 3.2 157.3 1.0 O B:GLY98 3.6 168.1 1.0 O A:ILE97 3.8 131.0 1.0 K A:K1002 3.9 78.0 0.2 O B:ILE97 3.9 119.6 1.0 C B:GLY98 4.0 157.9 1.0 C A:GLY98 4.1 153.9 1.0 O A:TYR99 4.4 174.7 1.0 C B:TYR99 4.5 155.6 1.0 O B:TYR99 4.5 172.1 1.0 C A:TYR99 4.5 157.4 1.0 N B:TYR99 4.6 150.2 1.0 CA B:TYR99 4.6 130.4 1.0 CA B:GLY98 4.7 149.7 1.0 CA A:TYR99 4.8 139.0 1.0 N A:TYR99 4.9 145.4 1.0 CA A:GLY98 5.0 159.6 1.0 N A:GLY100 5.0 173.8 1.0 C A:ILE97 5.0 142.0 1.0 C B:ILE97 5.0 119.2 1.0 N B:GLY100 5.0 170.1 1.0

C.Fagnen, L.Bannwarth, I.Oubella, D.Zuniga, A.Haouz, E.Forest, R.Scala, S.Bendahhou, R.De Zorzi, D.Perahia, C.Venien-Bryan. Integrative Study of the Structural and Dynamical Properties of A KIRBAC3.1 Mutant: Functional Implication of A Highly Conserved Tryptophan in the Transmembrane Domain. Int J Mol Sci V. 23 2021.
ISSN: ESSN 1422-0067
PubMed: 35008764
DOI: 10.3390/IJMS23010335