Potassium in PDB 7bt2: Crystal Structure of the SERCA2A in the E2.Atp State

All present enzymatic activity of Crystal Structure of the SERCA2A in the E2.Atp State:
7.2.2.10;

The structure of Crystal Structure of the SERCA2A in the E2.Atp State, PDB code: 7bt2 was solved by Y.Kabashima, H.Ogawa, R.Nakajima, C.Toyoshima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	14.99 / 3.00
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	121.604, 270.382, 97.340, 90.00, 90.00, 90.00
R / Rfree (%)	19.2 / 22.2

The binding sites of Potassium atom in the Crystal Structure of the SERCA2A in the E2.Atp State (pdb code 7bt2). 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 Crystal Structure of the SERCA2A in the E2.Atp State, PDB code: 7bt2:

Potassium binding site 1 out of 1 in the Crystal Structure of the SERCA2A in the E2.Atp State


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of the SERCA2A in the E2.Atp State within 5.0Å range: probe atom residue distance (Å) B Occ A:K1002 b:66.7 occ:1.00 O A:ALA713 2.5 58.6 1.0 O A:LEU710 2.7 55.4 1.0 O A:LYS711 2.8 46.2 1.0 OE1 A:GLU731 2.8 57.4 1.0 C A:LYS711 3.2 52.1 1.0 OE2 A:GLU731 3.3 79.1 1.0 CD A:GLU731 3.3 61.0 1.0 CA A:LYS711 3.5 53.5 1.0 C A:ALA713 3.7 49.1 1.0 C A:LEU710 3.7 48.4 1.0 N A:GLY716 3.9 53.2 1.0 N A:LYS711 4.1 45.5 1.0 N A:LYS712 4.2 48.4 1.0 N A:ALA713 4.2 46.7 1.0 O A:GLU714 4.3 61.7 1.0 C A:GLU714 4.4 54.6 1.0 CA A:ALA713 4.5 44.2 1.0 C A:LYS712 4.5 52.1 1.0 O A:ALA729 4.5 61.8 1.0 CA A:GLY716 4.5 42.8 1.0 N A:GLU714 4.6 47.7 1.0 CG A:GLU731 4.7 48.1 1.0 CA A:GLU714 4.8 46.1 1.0 N A:ILE715 4.8 50.3 1.0 C A:ILE715 4.8 52.3 1.0 CB A:LYS711 4.8 53.8 1.0 O A:LYS712 4.9 60.9 1.0 CA A:LYS712 4.9 52.1 1.0 CA A:ILE715 4.9 47.6 1.0 CB A:ALA713 4.9 45.7 1.0

Y.Kabashima, H.Ogawa, R.Nakajima, C.Toyoshima. What Atp Binding Does to the CA2+Pump and How Nonproductive Phosphoryl Transfer Is Prevented in the Absence of CA2. Proc.Natl.Acad.Sci.Usa V. 117 18448 2020.
ISSN: ESSN 1091-6490
PubMed: 32675243
DOI: 10.1073/PNAS.2006027117