Magnesium in PDB 8t2j: Structure of the Catalytic Domain of PPM1D/WIP1 Serine/Threonine Phosphatase

All present enzymatic activity of Structure of the Catalytic Domain of PPM1D/WIP1 Serine/Threonine Phosphatase:
3.1.3.16;

The structure of Structure of the Catalytic Domain of PPM1D/WIP1 Serine/Threonine Phosphatase, PDB code: 8t2j was solved by J.P.Kumar, D.Kosek, F.Dyda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.65 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.664, 59.93, 49.566, 90, 92.13, 90
R / Rfree (%)	17.5 / 21.9

The binding sites of Magnesium atom in the Structure of the Catalytic Domain of PPM1D/WIP1 Serine/Threonine Phosphatase (pdb code 8t2j). 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 Catalytic Domain of PPM1D/WIP1 Serine/Threonine Phosphatase, PDB code: 8t2j:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of the Catalytic Domain of PPM1D/WIP1 Serine/Threonine Phosphatase


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 Catalytic Domain of PPM1D/WIP1 Serine/Threonine Phosphatase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:24.4 occ:1.00 O A:HOH689 2.0 22.3 1.0 O A:HOH638 2.1 22.1 1.0 O A:HOH663 2.1 24.5 1.0 OD1 A:ASP105 2.1 20.7 1.0 O A:GLY106 2.2 21.0 1.0 O A:HOH639 2.2 23.6 1.0 CG A:ASP105 3.2 23.0 1.0 C A:GLY106 3.4 21.0 1.0 OD2 A:ASP105 3.8 22.6 1.0 MG A:MG502 3.8 24.0 1.0 N A:GLY106 3.9 21.9 1.0 O A:HOH645 3.9 26.3 1.0 O A:HOH686 3.9 30.9 1.0 O A:HOH661 4.0 28.1 1.0 C A:ASP105 4.0 23.5 1.0 O4 A:PEG503 4.1 37.0 1.0 OE1 A:GLU22 4.2 34.3 1.0 CA A:GLY106 4.2 21.3 1.0 OD1 A:ASP23 4.3 24.6 1.0 N A:HIS107 4.3 22.5 1.0 O A:HOH636 4.3 22.0 1.0 CB A:GLU22 4.4 25.9 1.0 OD1 A:ASN367 4.4 24.1 1.0 O A:ASP105 4.4 22.6 1.0 CA A:HIS107 4.4 23.3 1.0 CB A:ASP105 4.4 22.8 1.0 CB A:HIS107 4.5 24.9 1.0 CA A:ASP105 4.5 21.6 1.0 OD1 A:ASP366 4.6 23.4 1.0 O A:HOH699 4.7 30.9 1.0 NH1 A:ARG18 4.8 35.6 1.0 C4 A:PEG503 4.9 49.4 1.0 C A:GLU22 4.9 26.3 1.0 O A:GLU22 5.0 23.2 1.0

Magnesium binding site 2 out of 2 in the Structure of the Catalytic Domain of PPM1D/WIP1 Serine/Threonine Phosphatase


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 Catalytic Domain of PPM1D/WIP1 Serine/Threonine Phosphatase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg502 b:24.0 occ:1.00 OD2 A:ASP105 2.0 22.6 1.0 O A:HOH661 2.1 28.1 1.0 OD1 A:ASP314 2.1 19.2 1.0 O A:HOH636 2.1 22.0 1.0 OD2 A:ASP366 2.2 26.1 1.0 O A:HOH639 2.2 23.6 1.0 CG A:ASP105 3.0 23.0 1.0 CG A:ASP314 3.1 27.5 1.0 CG A:ASP366 3.2 25.3 1.0 OD1 A:ASP105 3.3 20.7 1.0 OD2 A:ASP314 3.4 31.2 1.0 OD1 A:ASP366 3.5 23.4 1.0 MG A:MG501 3.8 24.4 1.0 O A:HOH689 3.9 22.3 1.0 O A:HOH686 3.9 30.9 1.0 O A:HOH635 4.1 21.9 1.0 N A:GLY315 4.1 19.6 1.0 O A:HOH681 4.2 29.2 1.0 O A:HOH652 4.2 26.9 1.0 CB A:ASP105 4.3 22.8 1.0 O A:ASN367 4.3 21.2 1.0 OD1 A:ASP23 4.4 24.6 1.0 CB A:ASP314 4.4 23.2 1.0 O A:HOH638 4.5 22.1 1.0 N A:ASP314 4.5 22.9 1.0 CB A:ASP366 4.5 20.9 1.0 C A:ASP314 4.7 24.1 1.0 CA A:ASP314 4.7 24.7 1.0 CB A:SER313 4.9 23.8 1.0

J.P.Kumar, D.Kosek, F.Dyda. Structure of the Catalytic Domain of PPM1D/WIP1 Serine/Threonine Phosphatase To Be Published.