Magnesium in PDB 4fl5: Crystal Structure of Human 14-3-3 Sigma in Complex with A Tau-Protein Peptide Surrounding PS214

The structure of Crystal Structure of Human 14-3-3 Sigma in Complex with A Tau-Protein Peptide Surrounding PS214, PDB code: 4fl5 was solved by B.Schumacher, C.Ottmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.64 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	62.690, 70.080, 128.130, 90.00, 90.00, 90.00
R / Rfree (%)	15.6 / 21.2

The structure of Crystal Structure of Human 14-3-3 Sigma in Complex with A Tau-Protein Peptide Surrounding PS214 also contains other interesting chemical elements:

Chlorine	(Cl)	2 atoms
Calcium	(Ca)	6 atoms

The binding sites of Magnesium atom in the Crystal Structure of Human 14-3-3 Sigma in Complex with A Tau-Protein Peptide Surrounding PS214 (pdb code 4fl5). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of Human 14-3-3 Sigma in Complex with A Tau-Protein Peptide Surrounding PS214, PDB code: 4fl5:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Crystal Structure of Human 14-3-3 Sigma in Complex with A Tau-Protein Peptide Surrounding PS214


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Human 14-3-3 Sigma in Complex with A Tau-Protein Peptide Surrounding PS214 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg303 b:17.7 occ:1.00 O A:HOH627 1.6 27.8 1.0 O A:HOH629 1.9 64.6 1.0 OXT A:THR231 2.3 27.4 1.0 O A:HOH626 2.4 44.6 1.0 O A:THR228 2.4 20.6 1.0 O A:HOH637 2.9 47.6 1.0 C A:THR231 3.4 25.1 1.0 C A:THR228 3.5 17.4 1.0 OG1 A:THR228 3.7 21.3 0.5 O A:THR231 3.9 26.8 1.0 CG2 A:THR228 4.2 20.4 0.5 CA A:THR228 4.2 16.4 0.5 CA A:THR228 4.2 17.0 0.5 CB A:THR228 4.6 16.9 0.5 N A:LEU229 4.6 14.9 1.0 N A:THR231 4.6 20.0 1.0 O A:HOH638 4.6 35.7 1.0 CA A:THR231 4.7 22.6 1.0 O A:LEU229 4.7 15.5 1.0 C A:LEU229 4.8 15.5 1.0 CA A:LEU229 4.8 15.1 0.4 CA A:LEU229 4.8 14.6 0.6 CB A:THR228 4.8 17.5 0.5

Magnesium binding site 2 out of 4 in the Crystal Structure of Human 14-3-3 Sigma in Complex with A Tau-Protein Peptide Surrounding PS214


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Human 14-3-3 Sigma in Complex with A Tau-Protein Peptide Surrounding PS214 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg304 b:51.0 occ:1.00 O A:HOH633 2.3 30.5 0.5 OE1 A:GLU86 2.3 21.7 0.4 OE2 A:GLU89 2.3 16.7 1.0 O A:HOH634 2.3 24.5 1.0 OE2 A:GLU86 2.8 10.7 0.4 CD A:GLU86 2.9 17.3 0.4 CD A:GLU89 3.4 15.4 1.0 O A:HOH633 3.9 18.7 0.5 CG A:GLU89 4.2 13.4 1.0 NH1 A:ARG85 4.3 18.4 1.0 OE1 A:GLU89 4.3 12.7 1.0 CG A:GLU86 4.4 15.5 0.4 CG A:GLU86 4.5 12.4 0.6 CB A:GLU89 4.7 11.1 1.0 OE1 A:GLN93 4.7 15.5 1.0 NE2 A:GLN93 4.9 16.9 1.0

Magnesium binding site 3 out of 4 in the Crystal Structure of Human 14-3-3 Sigma in Complex with A Tau-Protein Peptide Surrounding PS214


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Human 14-3-3 Sigma in Complex with A Tau-Protein Peptide Surrounding PS214 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg301 b:32.9 occ:1.00 O B:HOH469 2.4 40.6 1.0 O B:HOH518 2.5 25.3 1.0 O B:HOH611 2.9 26.9 1.0 O B:HOH489 4.3 33.4 1.0 O B:HOH471 4.4 18.9 1.0 OD1 B:ASP204 4.6 15.9 1.0 OD2 B:ASP204 4.7 19.3 1.0

Magnesium binding site 4 out of 4 in the Crystal Structure of Human 14-3-3 Sigma in Complex with A Tau-Protein Peptide Surrounding PS214


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of Human 14-3-3 Sigma in Complex with A Tau-Protein Peptide Surrounding PS214 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg302 b:32.1 occ:1.00 OE2 B:GLU2 2.5 6.2 0.3 O B:HOH449 2.8 40.9 1.0 OG B:SER5 2.8 14.2 1.0 O B:HOH481 2.9 24.4 1.0 N B:SER5 3.6 12.3 1.0 CB B:GLU2 3.6 13.3 0.7 CB B:ALA4 3.7 14.3 1.0 CD B:GLU2 3.7 10.1 0.3 CB B:GLU2 3.8 11.8 0.3 CG B:GLU2 4.0 14.3 0.7 CB B:SER5 4.0 10.2 1.0 CA B:SER5 4.2 11.9 1.0 C B:ALA4 4.2 13.3 1.0 CA B:ALA4 4.4 12.8 1.0 CG B:GLU2 4.4 10.0 0.3 O B:HOH428 4.6 16.1 1.0 N B:ALA4 4.6 12.0 1.0 OE1 B:GLU2 4.7 11.6 0.3 CD B:GLU2 4.7 17.8 0.7

Y.Joo, B.Schumacher, M.Bartel, C.Smet-Nocca, A.Jang, H.S.Choi, N.L.Jeon, H.S.Kim, I.Landrieu, Y.H.Suh, C.Ottmann. 14-3-3 Binding to Tau Causes Tubulin Instability and Impairs Axon Development: Structural Basis and Functional Consequences of 14-3-3/Tau Interaction To Be Published.