Magnesium in PDB 7b13: 14-3-3SIGMA in Complex with SHN3PS542 Phosphopeptide Crystal Structure

The structure of 14-3-3SIGMA in Complex with SHN3PS542 Phosphopeptide Crystal Structure, PDB code: 7b13 was solved by L.Soini, S.Leysen, J.Davis, C.Ottmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.21 / 1.37
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	82.76, 112.83, 62.93, 90, 90, 90
R / Rfree (%)	15 / 17

The binding sites of Magnesium atom in the 14-3-3SIGMA in Complex with SHN3PS542 Phosphopeptide Crystal Structure (pdb code 7b13). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the 14-3-3SIGMA in Complex with SHN3PS542 Phosphopeptide Crystal Structure, PDB code: 7b13:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the 14-3-3SIGMA in Complex with SHN3PS542 Phosphopeptide Crystal Structure


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of 14-3-3SIGMA in Complex with SHN3PS542 Phosphopeptide Crystal Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:11.7 occ:0.50 O A:HOH649 2.3 37.9 1.0 OE1 A:GLU2 2.5 17.1 1.0 O A:HOH448 2.6 17.1 1.0 O A:HOH685 2.6 31.5 1.0 CD A:GLU2 3.5 16.0 1.0 OE2 A:GLU2 3.8 16.3 1.0 HA A:GLU2 4.0 13.0 1.0 H A:ARG3 4.2 13.1 1.0 O A:HOH620 4.4 16.1 1.0 O A:HOH768 4.5 18.1 1.0 CG A:GLU2 4.7 13.4 1.0 O A:HOH683 4.7 42.2 1.0 HB3 A:GLU2 4.8 15.6 1.0 CA A:GLU2 4.9 10.8 1.0 HG2 A:GLU2 5.0 16.1 1.0 N A:ARG3 5.0 10.9 1.0 O A:HOH515 5.0 26.1 1.0

Magnesium binding site 2 out of 4 in the 14-3-3SIGMA in Complex with SHN3PS542 Phosphopeptide Crystal Structure


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of 14-3-3SIGMA in Complex with SHN3PS542 Phosphopeptide Crystal Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:15.2 occ:1.00 OE1 A:GLU35 2.2 17.9 1.0 O A:HOH591 2.2 28.7 1.0 O A:GLU110 2.3 18.6 1.0 O A:HOH614 2.4 24.4 1.0 OE2 A:GLU35 2.7 29.3 1.0 CD A:GLU35 2.8 24.6 1.0 H A:GLY112 3.5 22.6 1.0 C A:GLU110 3.6 16.1 1.0 HB3 A:GLU110 3.8 19.3 0.5 HA A:ALA111 3.9 16.9 1.0 HB3 A:GLU110 4.0 18.3 0.5 N A:GLY112 4.1 18.8 1.0 HA A:GLU110 4.3 17.1 0.5 CG A:GLU35 4.3 18.5 1.0 HA A:GLU110 4.3 17.4 0.5 HA3 A:GLY112 4.4 24.6 1.0 CA A:GLU110 4.4 14.5 0.5 CA A:GLU110 4.4 14.3 0.5 O A:HOH551 4.5 29.3 1.0 N A:ALA111 4.5 14.9 1.0 HG2 A:GLU35 4.5 22.2 1.0 CA A:ALA111 4.6 14.1 1.0 CB A:GLU110 4.6 16.1 0.5 HG3 A:GLU35 4.6 22.2 1.0 OE1 A:GLU110 4.7 20.6 0.5 O A:HOH663 4.7 37.9 1.0 CB A:GLU110 4.7 15.2 0.5 C A:ALA111 4.8 15.0 1.0 CA A:GLY112 4.8 20.5 1.0

Magnesium binding site 3 out of 4 in the 14-3-3SIGMA in Complex with SHN3PS542 Phosphopeptide Crystal Structure


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of 14-3-3SIGMA in Complex with SHN3PS542 Phosphopeptide Crystal Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg303 b:83.9 occ:1.00 O A:HOH661 2.8 19.9 1.0 HD1 A:TYR84 3.0 15.0 1.0 HD2 A:LYS87 3.0 20.5 0.6 HD3 A:LYS87 3.1 22.6 0.4 HD2 A:LYS87 3.2 22.6 0.4 HA A:TYR84 3.4 12.7 1.0 HD3 A:LYS87 3.6 20.5 0.6 CD A:LYS87 3.6 18.8 0.4 HB2 A:TYR84 3.7 14.9 1.0 CD A:LYS87 3.7 17.1 0.6 CD1 A:TYR84 3.7 12.5 1.0 O A:HOH736 3.7 25.8 1.0 HB2 A:LYS87 3.9 15.5 0.6 HB2 A:LYS87 3.9 18.0 0.4 HZ2 A:LYS87 4.0 30.8 0.4 CA A:TYR84 4.1 10.6 1.0 HB3 A:LYS87 4.2 15.5 0.6 CB A:TYR84 4.2 12.4 1.0 HB3 A:LYS87 4.2 18.0 0.4 HZ1 A:LYS87 4.2 30.8 0.4 CG A:TYR84 4.3 11.2 1.0 HB3 A:GLU83 4.4 14.3 1.0 CB A:LYS87 4.4 12.9 0.6 CB A:LYS87 4.4 15.0 0.4 NZ A:LYS87 4.5 25.6 0.4 N A:TYR84 4.5 10.0 1.0 HE2 A:LYS87 4.6 26.8 0.6 CG A:LYS87 4.6 17.8 0.4 CG A:LYS87 4.6 15.8 0.6 O A:GLU83 4.6 11.9 1.0 CE A:LYS87 4.7 23.1 0.4 CE1 A:TYR84 4.7 12.3 1.0 HE1 A:TYR84 4.7 14.8 1.0 C A:GLU83 4.7 10.0 1.0 CE A:LYS87 4.7 22.3 0.6 H A:TYR84 4.9 12.1 1.0 HZ3 A:LYS87 4.9 32.4 0.6 HG3 A:LYS87 4.9 18.9 0.6

Magnesium binding site 4 out of 4 in the 14-3-3SIGMA in Complex with SHN3PS542 Phosphopeptide Crystal Structure


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of 14-3-3SIGMA in Complex with SHN3PS542 Phosphopeptide Crystal Structure within 5.0Å range: probe atom residue distance (Å) B Occ P:Mg601 b:27.2 occ:1.00 HD21 A:ASN175 2.3 13.1 1.0 O3P P:SEP542 2.8 12.3 1.0 C P:MET543 3.0 25.7 1.0 O A:HOH622 3.0 25.5 1.0 HB3 P:SEP542 3.0 19.0 1.0 ND2 A:ASN175 3.1 10.9 1.0 O P:MET543 3.2 24.5 1.0 H P:MET543 3.2 25.0 0.6 HA P:MET543 3.2 33.1 0.5 N P:MET543 3.2 20.9 1.0 HA P:PRO544 3.3 37.5 1.0 N P:PRO544 3.3 29.7 1.0 HH A:TYR130 3.3 15.5 1.0 H P:MET543 3.3 25.0 0.5 CA P:MET543 3.3 27.6 0.5 HD22 A:ASN175 3.5 13.1 1.0 HB3 P:PRO544 3.5 40.5 1.0 HD3 P:PRO544 3.5 38.9 1.0 CA P:MET543 3.5 26.6 0.6 OG P:SEP542 3.6 12.9 1.0 OH A:TYR130 3.7 12.9 1.0 CA P:PRO544 3.7 31.3 1.0 HZ1 A:LYS122 3.7 18.4 1.0 CB P:SEP542 3.7 15.8 1.0 C P:SEP542 3.7 20.0 1.0 P P:SEP542 3.8 12.4 1.0 HA P:MET543 3.8 32.0 0.6 HH22 A:ARG129 3.8 12.8 1.0 CD P:PRO544 3.9 32.4 1.0 CG A:ASN175 3.9 12.0 1.0 OD1 A:ASN175 4.0 12.2 1.0 CB P:PRO544 4.0 33.8 1.0 OD2 A:ASP126 4.2 11.9 1.0 O P:SEP542 4.3 20.4 1.0 O2P P:SEP542 4.3 14.7 1.0 CA P:SEP542 4.3 20.9 1.0 NH2 A:ARG129 4.5 10.7 1.0 NZ A:LYS122 4.5 15.4 1.0 HH21 A:ARG129 4.5 12.8 1.0 HZ3 A:LYS122 4.5 18.4 1.0 HB2 P:SEP542 4.5 19.0 1.0 CG A:ASP126 4.6 10.3 1.0 CG P:PRO544 4.7 34.3 1.0 HD2 P:PRO544 4.7 38.9 1.0 HA P:SEP542 4.7 25.0 1.0 HG3 A:LYS49 4.7 32.7 1.0 OD1 A:ASP126 4.8 10.5 1.0 CB P:MET543 4.8 31.5 0.5 O A:HOH432 4.8 29.8 1.0 HB2 P:PRO544 4.9 40.5 1.0 CB P:MET543 4.9 30.9 0.6 HB3 P:MET543 4.9 37.1 0.6 HG2 P:MET543 5.0 35.2 0.5 HB3 A:ASP126 5.0 11.2 1.0 HG3 P:PRO544 5.0 41.2 1.0

L.Soini, S.Leysen, J.Davis, C.Ottmann. 14-3-3 Sigma in Complex with Phosphopeptides To Be Published.