Magnesium in PDB 7obs: Crystal Structure of 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide

All present enzymatic activity of Crystal Structure of 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide:
2.7.10.2; 2.7.11.1;

The structure of Crystal Structure of 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide, PDB code: 7obs was solved by F.Centorrino, B.Andlovic, C.Ottmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.36 / 1.80
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	82.612, 111.816, 62.713, 90, 90, 90
R / Rfree (%)	14.6 / 18.9

The structure of Crystal Structure of 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Magnesium atom in the Crystal Structure of 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide (pdb code 7obs). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide, PDB code: 7obs:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Crystal Structure of 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide


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 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:3.7 occ:1.00 O A:HOH738 3.0 19.5 1.0 HD2 A:LYS87 3.0 22.5 1.0 HA A:TYR84 3.1 7.3 1.0 O A:HOH639 3.2 13.3 1.0 HD1 A:TYR84 3.2 5.1 1.0 HB2 A:LYS87 3.3 11.6 1.0 HB3 A:GLU83 3.6 7.0 1.0 HB2 A:TYR84 3.8 5.2 1.0 CA A:TYR84 3.8 6.1 1.0 HB3 A:LYS87 3.9 11.6 1.0 CD A:LYS87 3.9 18.8 1.0 O A:GLU83 4.0 6.3 1.0 CB A:LYS87 4.0 9.7 1.0 N A:TYR84 4.0 5.1 1.0 C A:GLU83 4.0 7.2 1.0 CD1 A:TYR84 4.1 4.2 1.0 HD3 A:LYS87 4.1 22.5 1.0 CB A:TYR84 4.3 4.3 1.0 CB A:GLU83 4.4 5.8 1.0 HB2 A:GLU83 4.4 7.0 1.0 CG A:LYS87 4.4 10.0 1.0 H A:TYR84 4.5 6.2 1.0 O A:HOH483 4.5 10.9 1.0 HZ2 A:LYS87 4.5 48.8 1.0 HG3 A:LYS87 4.6 12.0 1.0 HZ3 A:LYS87 4.6 48.8 1.0 CG A:TYR84 4.6 4.4 1.0 O A:HOH776 4.8 30.4 1.0 H A:LYS87 4.9 6.3 1.0 CA A:GLU83 4.9 4.8 1.0 NZ A:LYS87 4.9 40.6 1.0

Magnesium binding site 2 out of 3 in the Crystal Structure of 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide


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 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg303 b:10.7 occ:0.64 O A:HOH443 2.0 34.8 1.0 O A:HOH432 2.1 20.6 1.0 O A:HOH701 2.1 29.2 1.0 O A:HOH593 2.2 31.0 1.0 OE2 A:GLU89 2.3 10.4 1.0 O A:HOH659 2.4 29.5 1.0 CD A:GLU89 3.3 7.6 1.0 HG2 A:GLU86 3.7 13.3 1.0 HG2 A:GLU89 3.7 7.4 1.0 HH12 A:ARG85 3.7 14.1 1.0 CG A:GLU89 4.1 6.2 1.0 HE22 A:GLN93 4.1 12.9 1.0 O A:HOH462 4.2 23.6 1.0 HH11 A:ARG85 4.2 14.1 1.0 OE1 A:GLU89 4.2 6.0 1.0 HB3 A:GLU89 4.2 7.0 1.0 NH1 A:ARG85 4.3 11.7 1.0 HA A:GLU86 4.4 5.8 1.0 O A:HOH519 4.4 22.6 1.0 O A:HOH697 4.5 28.3 1.0 OE1 A:GLN93 4.5 7.1 1.0 CG A:GLU86 4.6 11.1 1.0 HG1 A:THR90 4.6 14.3 1.0 NE2 A:GLN93 4.7 10.8 1.0 CB A:GLU89 4.7 5.8 1.0 HB3 A:GLU86 4.8 9.4 1.0 HG3 A:GLU89 4.9 7.4 1.0 O A:HOH421 4.9 25.9 1.0 OG1 A:THR90 5.0 12.0 1.0

Magnesium binding site 3 out of 3 in the Crystal Structure of 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide


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 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg304 b:9.9 occ:0.50 OE1 A:GLU2 2.4 7.3 1.0 O A:HOH454 2.6 7.0 1.0 O A:HOH682 2.6 27.2 1.0 O A:HOH696 2.7 27.3 1.0 CD A:GLU2 3.4 8.7 1.0 OE2 A:GLU2 3.9 8.6 1.0 HA A:GLU2 4.0 5.8 1.0 H A:ARG3 4.1 5.7 1.0 O A:HOH629 4.3 6.6 1.0 O A:HOH777 4.5 8.5 1.0 HB3 A:GLU2 4.6 7.4 1.0 CG A:GLU2 4.7 4.3 1.0 CA A:GLU2 4.8 4.8 1.0 CB A:GLU2 4.9 6.2 1.0 N A:ARG3 4.9 4.7 1.0 HG2 A:GLU2 5.0 5.1 1.0 O A:HOH442 5.0 14.3 1.0

B.Andlovic, G.Heilmann, S.Ninck, S.Andrei, F.Centorrino, Y.Higuchi, N.Kato, L.Brunsveld, S.Menninger, A.Choidas, A.Wolf, M.Kaiser, J.Eickhoff, C.Ottmann. Inf Alpha Primes Ovarian Cancer Cells For Fusicoccin-Induced Cell Death Via Stabilization of 14-3-3 Protein-Protein Interactions To Be Published.