Potassium in PDB 4j2t: Inhibitor-Bound CA2+ Atpase

All present enzymatic activity of Inhibitor-Bound CA2+ Atpase:
3.6.3.8;

The structure of Inhibitor-Bound CA2+ Atpase, PDB code: 4j2t was solved by E.S.Paulsen, J.Villadsen, E.Tenori, H.Liu, M.A.Lie, D.F.Bonde, M.Bublitz, C.Olesen, H.E.Autzen, I.Dach, P.Sehgal, J.V.Moller, B.Schiott, P.Nissen, S.B.Christensen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.72 / 3.20
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	70.900, 70.900, 587.600, 90.00, 90.00, 90.00
R / Rfree (%)	26 / 28.6

The binding sites of Potassium atom in the Inhibitor-Bound CA2+ Atpase (pdb code 4j2t). 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 Inhibitor-Bound CA2+ Atpase, PDB code: 4j2t:

Potassium binding site 1 out of 1 in the Inhibitor-Bound CA2+ Atpase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Inhibitor-Bound CA2+ Atpase within 5.0Å range: probe atom residue distance (Å) B Occ A:K1003 b:78.9 occ:1.00 O A:HOH1101 2.8 60.4 1.0 OE2 A:GLU732 3.0 76.2 1.0 O A:ALA714 3.1 62.4 1.0 OE1 A:GLU732 3.2 75.2 1.0 CD A:GLU732 3.4 77.1 1.0 O A:LYS712 3.4 61.3 1.0 O A:LEU711 3.6 64.6 1.0 C A:LYS712 3.7 60.6 1.0 CA A:LYS712 4.0 60.1 1.0 O A:GLU715 4.1 67.8 1.0 C A:ALA714 4.4 63.3 1.0 N A:LYS713 4.5 69.3 1.0 OE1 A:GLN244 4.6 0.8 1.0 C A:GLU715 4.6 68.2 1.0 C A:LEU711 4.6 61.2 1.0 CG A:GLU732 4.6 76.2 1.0 O A:ALA730 4.7 68.1 1.0 N A:ALA714 4.8 60.9 1.0 N A:GLY717 4.8 58.2 1.0 N A:LYS712 4.8 58.3 1.0 C A:LYS713 4.9 74.6 1.0 CG A:LYS712 4.9 66.5 1.0 CA A:LYS713 5.0 72.3 1.0

E.S.Paulsen, J.Villadsen, E.Tenori, H.Liu, D.F.Bonde, M.A.Lie, M.Bublitz, C.Olesen, H.E.Autzen, I.Dach, P.Sehgal, P.Nissen, J.V.Moller, B.Schiott, S.B.Christensen. Water-Mediated Interactions Influence the Binding of Thapsigargin to Sarco/Endoplasmic Reticulum Calcium Adenosinetriphosphatase. J.Med.Chem. V. 56 3609 2013.
ISSN: ISSN 0022-2623
PubMed: 23574308
DOI: 10.1021/JM4001083