Potassium in PDB 6hef: Room Temperature Structure of the (Sr)CA2+-Atpase CA2-E1-Caamppcp Form

Protein crystallography data

The structure of Room Temperature Structure of the (Sr)CA2+-Atpase CA2-E1-Caamppcp Form, PDB code: 6hef was solved by S.Hjorth-Jensen, T.L.M.Sorensen, E.Oksanen, J.L.Andersen, C.Olesen, J.V.Moller, P.Nissen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.04 / 3.54
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 165.840, 77.770, 152.220, 90.00, 109.28, 90.00
R / Rfree (%) 22.3 / 25.7

Other elements in 6hef:

The structure of Room Temperature Structure of the (Sr)CA2+-Atpase CA2-E1-Caamppcp Form also contains other interesting chemical elements:

Calcium (Ca) 3 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Room Temperature Structure of the (Sr)CA2+-Atpase CA2-E1-Caamppcp Form (pdb code 6hef). 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 Room Temperature Structure of the (Sr)CA2+-Atpase CA2-E1-Caamppcp Form, PDB code: 6hef:

Potassium binding site 1 out of 1 in 6hef

Go back to Potassium Binding Sites List in 6hef
Potassium binding site 1 out of 1 in the Room Temperature Structure of the (Sr)CA2+-Atpase CA2-E1-Caamppcp Form


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Room Temperature Structure of the (Sr)CA2+-Atpase CA2-E1-Caamppcp Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1005

b:0.3
occ:1.00
O A:LYS712 3.1 66.2 1.0
O A:ALA714 3.7 66.5 1.0
OE2 A:GLU732 4.1 73.8 1.0
C A:LYS712 4.3 67.2 1.0
O A:LYS713 4.5 72.0 1.0
O A:GLU715 4.6 65.0 1.0
C A:LYS713 4.7 68.0 1.0
C A:ALA714 4.7 67.4 1.0
CA A:LYS713 4.9 67.6 1.0

Reference:

T.L.M.Sorensen, S.J.Hjorth-Jensen, E.Oksanen, J.L.Andersen, C.Olesen, J.V.Moller, P.Nissen. Membrane-Protein Crystals For Neutron Diffraction. Acta Crystallogr D Struct V. 74 1208 2018BIOL.
ISSN: ISSN 2059-7983
PubMed: 30605135
DOI: 10.1107/S2059798318012561
Page generated: Mon Dec 14 00:40:17 2020

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