Potassium in PDB 4qe9: Open Mthk Pore Structure Soaked in 10 Mm BA2+/100 Mm K+

The structure of Open Mthk Pore Structure Soaked in 10 Mm BA2+/100 Mm K+, PDB code: 4qe9 was solved by R.Guo, W.Zeng, H.Cui, L.Chen, S.Ye, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.50 / 2.15
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	61.005, 61.005, 44.950, 90.00, 90.00, 90.00
R / Rfree (%)	19.8 / 25.7

The binding sites of Potassium atom in the Open Mthk Pore Structure Soaked in 10 Mm BA2+/100 Mm K+ (pdb code 4qe9). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 6 binding sites of Potassium where determined in the Open Mthk Pore Structure Soaked in 10 Mm BA2+/100 Mm K+, PDB code: 4qe9:
Jump to Potassium binding site number: 1; 2; 3; 4; 5; 6;

Potassium binding site 1 out of 6 in the Open Mthk Pore Structure Soaked in 10 Mm BA2+/100 Mm K+


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Open Mthk Pore Structure Soaked in 10 Mm BA2+/100 Mm K+ within 5.0Å range: probe atom residue distance (Å) B Occ A:K201 b:47.9 occ:0.25 O A:TYR62 3.0 38.8 1.0 O A:GLY61 3.0 39.0 1.0 K A:K202 3.2 45.4 0.2 C A:TYR62 3.6 39.1 1.0 CA A:TYR62 4.1 38.8 1.0 C A:GLY61 4.2 39.1 1.0 N A:GLY63 4.3 39.1 1.0 CA A:GLY63 4.6 39.0 1.0 N A:TYR62 4.7 38.8 1.0

Potassium binding site 2 out of 6 in the Open Mthk Pore Structure Soaked in 10 Mm BA2+/100 Mm K+


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Open Mthk Pore Structure Soaked in 10 Mm BA2+/100 Mm K+ within 5.0Å range: probe atom residue distance (Å) B Occ A:K202 b:45.4 occ:0.25 O A:GLY61 2.8 39.0 1.0 O A:VAL60 3.0 38.4 1.0 K A:K203 3.1 42.0 0.2 K A:K201 3.2 47.9 0.2 C A:GLY61 3.7 39.1 1.0 C A:VAL60 4.1 38.6 1.0 CA A:GLY61 4.2 38.8 1.0 N A:TYR62 4.6 38.8 1.0 N A:GLY61 4.6 39.2 1.0 CA A:TYR62 4.9 38.8 1.0

Potassium binding site 3 out of 6 in the Open Mthk Pore Structure Soaked in 10 Mm BA2+/100 Mm K+


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Open Mthk Pore Structure Soaked in 10 Mm BA2+/100 Mm K+ within 5.0Å range: probe atom residue distance (Å) B Occ A:K203 b:42.0 occ:0.25 O A:THR59 2.9 38.6 1.0 O A:VAL60 2.9 38.4 1.0 K A:K202 3.1 45.4 0.2 K A:K204 3.6 44.5 0.2 C A:VAL60 3.7 38.6 1.0 C A:THR59 4.0 39.1 1.0 CA A:VAL60 4.2 38.3 1.0 N A:VAL60 4.6 38.4 1.0 N A:GLY61 4.7 39.2 1.0

Potassium binding site 4 out of 6 in the Open Mthk Pore Structure Soaked in 10 Mm BA2+/100 Mm K+


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Open Mthk Pore Structure Soaked in 10 Mm BA2+/100 Mm K+ within 5.0Å range: probe atom residue distance (Å) B Occ A:K204 b:44.5 occ:0.25 OG1 A:THR59 2.8 40.2 1.0 O A:THR59 3.1 38.6 1.0 K A:K206 3.2 0.3 0.3 CB A:THR59 3.6 40.1 1.0 K A:K203 3.6 42.0 0.2 C A:THR59 4.0 39.1 1.0 CA A:THR59 4.5 39.1 1.0 CG2 A:THR59 4.8 42.5 1.0

Potassium binding site 5 out of 6 in the Open Mthk Pore Structure Soaked in 10 Mm BA2+/100 Mm K+


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 5 of Open Mthk Pore Structure Soaked in 10 Mm BA2+/100 Mm K+ within 5.0Å range: probe atom residue distance (Å) B Occ A:K205 b:94.1 occ:0.25 O A:HOH343 4.1 81.1 1.0 O A:HOH342 4.7 59.7 1.0

Potassium binding site 6 out of 6 in the Open Mthk Pore Structure Soaked in 10 Mm BA2+/100 Mm K+


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 6 of Open Mthk Pore Structure Soaked in 10 Mm BA2+/100 Mm K+ within 5.0Å range: probe atom residue distance (Å) B Occ A:K206 b:0.3 occ:0.25 O A:HOH341 2.8 50.3 1.0 K A:K204 3.2 44.5 0.2 OG1 A:THR59 3.6 40.2 1.0 CB A:THR59 4.7 40.1 1.0 CG2 A:THR59 5.0 42.5 1.0

R.Guo, W.Zeng, H.Cui, L.Chen, S.Ye. Ionic Interactions of BA2+ Blockades in the Mthk K+ Channel J.Gen.Physiol..
ISSN: ESSN 1540-7748