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Potassium in PDB 4nab: Structure of the (Sr)CA2+-Atpase Mutant E309Q in the CA2-E1-Mgamppcp Form

Enzymatic activity of Structure of the (Sr)CA2+-Atpase Mutant E309Q in the CA2-E1-Mgamppcp Form

All present enzymatic activity of Structure of the (Sr)CA2+-Atpase Mutant E309Q in the CA2-E1-Mgamppcp Form:
3.6.3.8;

Protein crystallography data

The structure of Structure of the (Sr)CA2+-Atpase Mutant E309Q in the CA2-E1-Mgamppcp Form, PDB code: 4nab was solved by M.Bublitz, J.D.Clausen, B.Arnou, C.Montigny, C.Jaxel, P.Nissen, J.V.Mueller, J.P.Andersen, M.Le Maire, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 67.01 / 3.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 167.010, 55.790, 161.790, 90.00, 109.29, 90.00
R / Rfree (%) 21.6 / 26.6

Other elements in 4nab:

The structure of Structure of the (Sr)CA2+-Atpase Mutant E309Q in the CA2-E1-Mgamppcp Form also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Structure of the (Sr)CA2+-Atpase Mutant E309Q in the CA2-E1-Mgamppcp Form (pdb code 4nab). 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 Structure of the (Sr)CA2+-Atpase Mutant E309Q in the CA2-E1-Mgamppcp Form, PDB code: 4nab:

Potassium binding site 1 out of 1 in 4nab

Go back to Potassium Binding Sites List in 4nab
Potassium binding site 1 out of 1 in the Structure of the (Sr)CA2+-Atpase Mutant E309Q in the CA2-E1-Mgamppcp Form


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of the (Sr)CA2+-Atpase Mutant E309Q in the CA2-E1-Mgamppcp Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1104

b:0.1
occ:1.00
 O A:ALA714 2.7 98.7 1.0
O A:LEU711 2.7 0.2 1.0
OE1 A:GLU732 2.8 96.3 1.0
OE2 A:GLU732 2.8 1.0 1.0
O A:HOH1202 2.8 94.3 1.0
CD A:GLU732 3.1 98.4 1.0
O A:LYS712 3.3 0.3 1.0
CA A:LYS712 3.4 0.6 1.0
C A:LYS712 3.4 0.8 1.0
C A:LEU711 3.5 0.3 1.0
C A:ALA714 3.7 91.4 1.0
N A:LYS712 3.8 0.9 1.0
N A:GLY717 4.0 78.6 1.0
N A:ALA714 4.2 90.0 1.0
O A:GLU715 4.2 79.3 1.0
N A:LYS713 4.2 0.6 1.0
C A:GLU715 4.4 82.1 1.0
CA A:ALA714 4.4 88.1 1.0
CA A:GLY717 4.5 79.6 1.0
CG A:GLU732 4.6 93.4 1.0
C A:LYS713 4.6 95.8 1.0
N A:GLU715 4.7 86.0 1.0
CA A:LEU711 4.7 97.6 1.0
CB A:LYS712 4.7 0.5 1.0
CB A:ALA714 4.8 71.3 1.0
CA A:GLU715 4.8 83.4 1.0
N A:ILE716 4.8 85.1 1.0
CA A:LYS713 4.9 0.2 1.0
C A:ILE716 4.9 79.0 1.0

Reference:

J.D.Clausen, M.Bublitz, B.Arnou, C.Montigny, C.Jaxel, J.V.Mller, P.Nissen, J.P.Andersen, M.Le Maire. Serca Mutant E309Q Binds Two Ca(2+) Ions But Adopts A Catalytically Incompetent Conformation. Embo J. V. 32 3231 2013.
ISSN: ISSN 0261-4189
PubMed: 24270570
DOI: 10.1038/EMBOJ.2013.250
Page generated: Sun Dec 13 23:45:51 2020

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