Potassium in PDB 2yfy: Serca in the HNE2 State Complexed with Debutanoyl Thapsigargin

All present enzymatic activity of Serca in the HNE2 State Complexed with Debutanoyl Thapsigargin:
3.6.3.8;

The structure of Serca in the HNE2 State Complexed with Debutanoyl Thapsigargin, PDB code: 2yfy was solved by Y.Sonntag, M.Musgaard, C.Olesen, B.Schiott, J.V.Moller, P.Nissen, L.Thogersen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	57.684 / 3.10
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	71.360, 71.360, 587.910, 90.00, 90.00, 90.00
R / Rfree (%)	23.93 / 27.75

The structure of Serca in the HNE2 State Complexed with Debutanoyl Thapsigargin also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Potassium atom in the Serca in the HNE2 State Complexed with Debutanoyl Thapsigargin (pdb code 2yfy). 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 Serca in the HNE2 State Complexed with Debutanoyl Thapsigargin, PDB code: 2yfy:

Potassium binding site 1 out of 1 in the Serca in the HNE2 State Complexed with Debutanoyl Thapsigargin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Serca in the HNE2 State Complexed with Debutanoyl Thapsigargin within 5.0Å range: probe atom residue distance (Å) B Occ A:K1996 b:0.6 occ:1.00 O A:GLU715 3.7 74.2 1.0 O A:ALA714 3.7 77.5 1.0 OE2 A:GLU732 3.8 87.8 1.0 OE1 A:GLN244 3.8 0.1 1.0 CD A:GLU732 3.9 84.6 1.0 O A:LYS712 3.9 72.5 1.0 OE1 A:GLU732 4.0 86.3 1.0 CB A:GLN244 4.2 0.6 1.0 CD A:GLN244 4.3 0.4 1.0 C A:GLU715 4.3 73.8 1.0 CG A:GLU732 4.5 77.8 1.0 C A:LYS712 4.7 74.7 1.0 CA A:GLU715 4.7 76.8 1.0 C A:ALA714 4.8 83.2 1.0 NE2 A:GLN244 4.8 0.2 1.0 CG A:GLN244 4.8 0.1 1.0 O A:LYS713 4.9 90.4 1.0 O A:LEU711 5.0 72.5 1.0

Y.Sonntag, M.Musgaard, C.Olesen, B.Schiott, J.V.Moller, P.Nissen, L.Thogersen. Mutual Adaptation of A Membrane Protein and Its Lipid Bilayer During Conformational Changes. Nat.Commun. V. 2 304 2011.
ISSN: ISSN 2041-1723
PubMed: 21556058
DOI: 10.1038/NCOMMS1307