Potassium in PDB 6hxb: SERCA2A From Pig Heart

All present enzymatic activity of SERCA2A From Pig Heart:
3.6.3.8;

The structure of SERCA2A From Pig Heart, PDB code: 6hxb was solved by A.Sitsel, J.L.Andersen, P.Nissen, C.Olesen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.72 / 4.00
Space group	P 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	116.995, 51.776, 125.604, 90.00, 106.13, 90.00
R / Rfree (%)	31 / 35.4

The structure of SERCA2A From Pig Heart also contains other interesting chemical elements:

Calcium

(Ca)

3 atoms

The binding sites of Potassium atom in the SERCA2A From Pig Heart (pdb code 6hxb). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the SERCA2A From Pig Heart, PDB code: 6hxb:

Potassium binding site 1 out of 1 in the SERCA2A From Pig Heart


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of SERCA2A From Pig Heart within 5.0Å range: probe atom residue distance (Å) B Occ A:K1005 b:0.4 occ:1.00 OE2 A:GLU731 2.8 0.2 1.0 O A:LEU710 2.8 0.9 1.0 O A:SER713 2.8 0.2 1.0 O A:LYS711 3.0 0.2 1.0 OE1 A:GLU731 3.0 0.5 1.0 CD A:GLU731 3.3 0.1 1.0 O A:GLU714 3.7 94.9 1.0 C A:LYS711 3.7 0.6 1.0 C A:LEU710 3.9 0.6 1.0 C A:SER713 3.9 0.0 1.0 CA A:LYS711 4.0 0.0 1.0 O A:ALA729 4.0 0.8 1.0 C A:GLU714 4.1 0.3 1.0 N A:GLY716 4.3 0.3 1.0 N A:LYS711 4.4 0.5 1.0 N A:ILE715 4.5 0.9 1.0 N A:SER713 4.6 0.1 1.0 C A:ILE715 4.6 0.5 1.0 CA A:ILE715 4.7 0.4 1.0 CA A:GLU714 4.7 0.0 1.0 CG A:GLU731 4.8 0.3 1.0 N A:GLU714 4.8 0.9 1.0 CA A:SER713 4.8 0.6 1.0 N A:LYS712 4.9 0.7 1.0 CA A:GLY716 4.9 0.3 1.0 C A:LYS712 5.0 0.8 1.0

A.Sitsel, J.De Raeymaecker, N.D.Drachmann, R.Derua, S.Smaardijk, J.L.Andersen, I.Vandecaetsbeek, J.Chen, M.De Maeyer, E.Waelkens, C.Olesen, P.Vangheluwe, P.Nissen. Structures of the Heart Specific SERCA2A CA2+-Atpase. Embo J. V. 38 2019.
ISSN: ESSN 1460-2075
PubMed: 30777856
DOI: 10.15252/EMBJ.2018100020