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Magnesium in PDB 3n5k: Structure of the (Sr)CA2+-Atpase E2-ALF4- Form

Enzymatic activity of Structure of the (Sr)CA2+-Atpase E2-ALF4- Form

All present enzymatic activity of Structure of the (Sr)CA2+-Atpase E2-ALF4- Form:
3.6.3.8;

Protein crystallography data

The structure of Structure of the (Sr)CA2+-Atpase E2-ALF4- Form, PDB code: 3n5k was solved by M.Bublitz, C.Olesen, H.Poulsen, J.P.Morth, J.V.Moller, P.Nissen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 72.00 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 101.930, 109.420, 276.092, 90.00, 90.00, 90.00
R / Rfree (%) 18.4 / 21.6

Other elements in 3n5k:

The structure of Structure of the (Sr)CA2+-Atpase E2-ALF4- Form also contains other interesting chemical elements:

Fluorine (F) 8 atoms
Aluminium (Al) 2 atoms
Potassium (K) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of the (Sr)CA2+-Atpase E2-ALF4- Form (pdb code 3n5k). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of the (Sr)CA2+-Atpase E2-ALF4- Form, PDB code: 3n5k:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3n5k

Go back to Magnesium Binding Sites List in 3n5k
Magnesium binding site 1 out of 2 in the Structure of the (Sr)CA2+-Atpase E2-ALF4- Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the (Sr)CA2+-Atpase E2-ALF4- Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2001

b:26.7
occ:1.00
F3 A:ALF2002 2.0 23.1 1.0
OD1 A:ASP703 2.2 30.0 1.0
O A:THR353 2.2 23.7 1.0
O A:HOH1279 2.2 23.0 1.0
OD2 A:ASP351 2.2 23.9 1.0
O A:HOH1366 2.3 21.1 1.0
CG A:ASP351 3.0 24.2 1.0
CG A:ASP703 3.2 27.2 1.0
OD1 A:ASP351 3.2 23.8 1.0
C A:THR353 3.3 26.5 1.0
AL A:ALF2002 3.5 24.9 1.0
F1 A:ALF2002 3.5 27.4 1.0
OD2 A:ASP703 3.6 29.7 1.0
O A:HOH1083 3.9 25.5 1.0
CA A:THR353 3.9 21.3 1.0
N A:THR353 4.0 21.7 1.0
CB A:THR353 4.0 19.1 1.0
OD2 A:ASP707 4.1 25.4 1.0
O A:GLY182 4.2 25.8 1.0
OG1 A:THR355 4.2 22.6 1.0
F2 A:ALF2002 4.3 23.4 1.0
O A:HOH1119 4.3 34.6 1.0
CB A:ASP351 4.4 21.3 1.0
N A:GLY354 4.4 25.0 1.0
N A:GLY704 4.5 20.6 1.0
CA A:GLY182 4.5 23.2 1.0
N A:ASP703 4.5 27.2 1.0
O A:HOH1365 4.5 23.3 1.0
CB A:ASP703 4.6 25.9 1.0
CG2 A:THR353 4.6 15.0 1.0
CA A:GLY354 4.7 24.7 1.0
C A:LYS352 4.8 23.4 1.0
C A:ASP703 4.8 23.1 1.0
C A:GLY182 4.8 27.3 1.0
CA A:ASP703 4.9 25.4 1.0
CA A:GLY704 4.9 18.6 1.0
N A:THR355 4.9 23.2 1.0

Magnesium binding site 2 out of 2 in 3n5k

Go back to Magnesium Binding Sites List in 3n5k
Magnesium binding site 2 out of 2 in the Structure of the (Sr)CA2+-Atpase E2-ALF4- Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of the (Sr)CA2+-Atpase E2-ALF4- Form within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg2001

b:28.4
occ:1.00
F3 B:ALF2002 2.0 23.6 1.0
O B:HOH1228 2.1 29.4 1.0
OD1 B:ASP703 2.2 28.1 1.0
OD2 B:ASP351 2.2 25.4 1.0
O B:HOH1226 2.2 27.0 1.0
O B:THR353 2.2 25.9 1.0
CG B:ASP351 3.1 26.1 1.0
CG B:ASP703 3.2 27.8 1.0
OD1 B:ASP351 3.3 22.7 1.0
C B:THR353 3.4 23.0 1.0
F1 B:ALF2002 3.4 28.6 1.0
AL B:ALF2002 3.5 24.9 1.0
OD2 B:ASP703 3.6 32.4 1.0
O B:HOH1096 3.9 31.4 1.0
CA B:THR353 4.0 22.4 1.0
CB B:THR353 4.0 23.9 1.0
OD2 B:ASP707 4.0 26.6 1.0
N B:THR353 4.0 26.4 1.0
OG1 B:THR355 4.2 26.4 1.0
O B:GLY182 4.3 22.6 1.0
F2 B:ALF2002 4.3 23.3 1.0
O B:HOH1240 4.3 37.6 1.0
CB B:ASP351 4.4 23.1 1.0
N B:GLY704 4.4 28.0 1.0
O B:HOH1311 4.5 22.3 1.0
N B:GLY354 4.5 24.6 1.0
N B:ASP703 4.5 30.0 1.0
CB B:ASP703 4.6 26.6 1.0
CA B:GLY182 4.6 25.6 1.0
CG2 B:THR353 4.6 20.4 1.0
C B:ASP703 4.8 31.4 1.0
CA B:GLY354 4.8 23.0 1.0
CA B:GLY704 4.8 22.8 1.0
C B:LYS352 4.8 25.7 1.0
CA B:ASP703 4.9 29.1 1.0
C B:GLY182 4.9 24.2 1.0
N B:THR355 4.9 26.1 1.0

Reference:

M.Bublitz, M.Musgaard, H.Poulsen, L.Thogersen, C.Olesen, B.Schiott, J.P.Morth, J.V.Moller, P.Nissen. Ion Pathways in the Sarcoplasmic Reticulum CA2+-Atpase. J.Biol.Chem. V. 288 10759 2013.
ISSN: ISSN 0021-9258
PubMed: 23400778
DOI: 10.1074/JBC.R112.436550
Page generated: Mon Dec 14 08:27:43 2020

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