Potassium in PDB 7n9k: KIRBAC3.1 L124M Mutant

The structure of KIRBAC3.1 L124M Mutant, PDB code: 7n9k was solved by T.A.Black, J.M.Gulbis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.08 / 2.72
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	106.577, 106.577, 89.597, 90, 90, 90
R / Rfree (%)	21.8 / 25

The binding sites of Potassium atom in the KIRBAC3.1 L124M Mutant (pdb code 7n9k). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 7 binding sites of Potassium where determined in the KIRBAC3.1 L124M Mutant, PDB code: 7n9k:
Jump to Potassium binding site number: 1; 2; 3; 4; 5; 6; 7;

Potassium binding site 1 out of 7 in the KIRBAC3.1 L124M Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of KIRBAC3.1 L124M Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:K506 b:59.1 occ:0.18 O A:GLY98 2.7 53.4 1.0 O A:TYR99 2.8 59.1 1.0 C A:TYR99 3.6 57.6 1.0 C A:GLY98 3.9 49.9 1.0 HA A:TYR99 4.0 76.7 1.0 CA A:TYR99 4.3 63.7 1.0 HA2 A:GLY100 4.3 95.5 1.0 HA3 A:GLY100 4.3 95.5 1.0 N A:GLY100 4.4 66.9 1.0 N A:TYR99 4.6 55.7 1.0 CA A:GLY100 4.6 79.4 1.0 HA3 A:GLY98 4.8 60.6 1.0

Potassium binding site 2 out of 7 in the KIRBAC3.1 L124M Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of KIRBAC3.1 L124M Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:K507 b:57.6 occ:0.14 O A:THR96 2.7 55.1 1.0 O A:ILE97 2.8 57.4 1.0 K A:K508 3.4 57.2 0.2 HA A:ILE97 3.5 65.9 1.0 C A:ILE97 3.5 54.6 1.0 C A:THR96 3.8 52.3 1.0 CA A:ILE97 4.0 54.7 1.0 HA3 A:GLY98 4.4 60.6 1.0 N A:ILE97 4.4 53.5 1.0 N A:GLY98 4.5 48.1 1.0 HB A:THR96 4.6 70.0 1.0 HG1 A:THR96 4.6 74.0 1.0 CA A:GLY98 4.9 50.3 1.0

Potassium binding site 3 out of 7 in the KIRBAC3.1 L124M Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of KIRBAC3.1 L124M Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:K508 b:57.2 occ:0.18 HG1 A:THR96 2.4 74.0 1.0 O A:THR96 2.9 55.1 1.0 OG1 A:THR96 2.9 61.5 1.0 HB A:THR96 3.2 70.0 1.0 K A:K507 3.4 57.6 0.1 CB A:THR96 3.6 58.1 1.0 C A:THR96 3.8 52.3 1.0 CA A:THR96 4.4 51.2 1.0 K A:K509 4.4 107.5 0.2 HA A:ILE97 4.5 65.9 1.0 O A:ALA95 4.6 54.8 1.0 HG21 A:THR96 4.8 57.0 1.0 CG2 A:THR96 4.8 47.3 1.0 N A:ILE97 4.8 53.5 1.0 HA A:THR96 5.0 61.7 1.0

Potassium binding site 4 out of 7 in the KIRBAC3.1 L124M Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of KIRBAC3.1 L124M Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:K509 b:107.5 occ:0.25 K A:K511 3.2 85.1 0.7 OG1 A:THR96 4.3 61.5 1.0 K A:K508 4.4 57.2 0.2 HG1 A:THR96 4.5 74.0 1.0 H41 A:OCT505 4.5 78.0 1.0 H42 A:OCT505 4.6 78.0 1.0

Potassium binding site 5 out of 7 in the KIRBAC3.1 L124M Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 5 of KIRBAC3.1 L124M Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:K510 b:68.4 occ:0.25 K A:K512 4.2 81.2 0.8 CG A:TYR132 4.7 39.6 1.0 CD1 A:TYR132 4.7 41.3 1.0 CD2 A:TYR132 4.8 38.2 1.0 CE1 A:TYR132 4.9 32.8 1.0 HB2 A:TYR132 4.9 39.6 1.0 CE2 A:TYR132 4.9 32.2 1.0 CZ A:TYR132 5.0 35.7 1.0 HD1 A:TYR132 5.0 49.8 1.0

Potassium binding site 6 out of 7 in the KIRBAC3.1 L124M Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 6 of KIRBAC3.1 L124M Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:K511 b:85.1 occ:0.68 K A:K509 3.2 107.5 0.2 HG21 A:THR96 3.6 57.0 1.0 SD A:MET124 3.7 76.9 1.0 HG23 A:THR96 3.8 57.0 1.0 HE1 A:MET124 3.9 92.3 1.0 OG1 A:THR96 4.0 61.5 1.0 CG2 A:THR96 4.1 47.3 1.0 CE A:MET124 4.4 76.7 1.0 H42 A:OCT505 4.4 78.0 1.0 H31 A:OCT505 4.5 70.9 1.0 O A:ALA95 4.5 54.8 1.0 H32 A:OCT505 4.5 70.9 1.0 HG2 A:MET121 4.6 78.1 0.5 HG1 A:THR96 4.6 74.0 1.0 CB A:THR96 4.7 58.1 1.0 HG3 A:MET121 4.7 78.1 0.5 H41 A:OCT505 4.8 78.0 1.0 HE2 A:MET121 4.8 69.7 0.5 C3 A:OCT505 4.9 58.9 1.0 C4 A:OCT505 4.9 64.8 1.0 HE2 A:MET124 5.0 92.3 1.0 HG22 A:THR96 5.0 57.0 1.0

Potassium binding site 7 out of 7 in the KIRBAC3.1 L124M Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 7 of KIRBAC3.1 L124M Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:K512 b:81.2 occ:0.85 H82 A:OCT505 2.8 61.0 1.0 HB1 A:ALA128 3.2 47.3 1.0 H81 A:OCT505 3.3 61.0 1.0 C8 A:OCT505 3.3 50.6 1.0 HB2 A:TYR132 3.9 39.6 1.0 CB A:ALA128 4.2 39.2 1.0 K A:K510 4.2 68.4 0.2 HB3 A:ALA128 4.4 47.3 1.0 O A:ALA128 4.6 47.5 1.0 HB2 A:ALA128 4.7 47.3 1.0 C7 A:OCT505 4.7 46.7 1.0 HD1 A:TYR132 4.7 49.8 1.0 C A:ALA128 4.8 44.3 1.0 CB A:TYR132 4.8 32.8 1.0 H71 A:OCT505 4.9 56.2 1.0 HB3 A:TYR132 5.0 39.6 1.0 CA A:ALA128 5.0 40.4 1.0

J.M.Gulbis, K.A.Black. Ion Currents Through Kir Potassium Channels Are Gated By Anionic Lipids. Nat Commun 2021.
ISSN: ESSN 2041-1723