Magnesium in PDB 7kpr: Structure of Wild-Type PPM1H Phosphatase at 3.1 Angstrom Resolution

All present enzymatic activity of Structure of Wild-Type PPM1H Phosphatase at 3.1 Angstrom Resolution:
3.1.3.16;

The structure of Structure of Wild-Type PPM1H Phosphatase at 3.1 Angstrom Resolution, PDB code: 7kpr was solved by A.R.Khan, D.Waschbusch, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.78 / 3.09
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	69.684, 102.16, 148.7, 90, 90, 90
R / Rfree (%)	19.6 / 22

The binding sites of Magnesium atom in the Structure of Wild-Type PPM1H Phosphatase at 3.1 Angstrom Resolution (pdb code 7kpr). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Structure of Wild-Type PPM1H Phosphatase at 3.1 Angstrom Resolution, PDB code: 7kpr:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Structure of Wild-Type PPM1H Phosphatase at 3.1 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Wild-Type PPM1H Phosphatase at 3.1 Angstrom Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:89.0 occ:1.00 O A:GLY152 2.5 88.0 1.0 OD1 A:ASP151 2.6 80.5 1.0 MG A:MG602 3.5 77.4 1.0 CG A:ASP151 3.7 79.0 1.0 C A:GLY152 3.8 83.6 1.0 O A:HOH705 3.8 82.6 1.0 O A:HOH704 3.8 77.4 1.0 OD1 A:ASP498 4.0 79.7 1.0 OE1 A:GLU93 4.0 93.3 1.0 OD2 A:ASP499 4.1 82.4 1.0 OD2 A:ASP151 4.1 81.5 1.0 CB A:GLU93 4.3 89.1 1.0 OD1 A:ASP94 4.3 83.6 1.0 N A:GLY152 4.5 79.1 1.0 NZ A:LYS88 4.6 81.6 1.0 CE A:LYS88 4.6 84.3 1.0 O A:HOH701 4.6 78.6 1.0 N A:HIS153 4.7 84.2 1.0 CA A:HIS153 4.7 85.3 1.0 CA A:GLY152 4.7 81.0 1.0 C A:ASP151 4.8 78.1 1.0 OD2 A:ASP498 4.8 82.7 1.0 CG A:ASP498 4.8 81.5 1.0 CB A:HIS153 4.9 84.8 1.0 CD A:GLU93 5.0 99.4 1.0

Magnesium binding site 2 out of 4 in the Structure of Wild-Type PPM1H Phosphatase at 3.1 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Wild-Type PPM1H Phosphatase at 3.1 Angstrom Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg602 b:77.4 occ:1.00 OD2 A:ASP498 1.9 82.7 1.0 O A:HOH701 2.0 78.6 1.0 O A:HOH704 2.0 77.4 1.0 OD2 A:ASP151 2.1 81.5 1.0 OD1 A:ASP437 2.6 79.5 1.0 CG A:ASP498 2.8 81.5 1.0 CG A:ASP151 2.9 79.0 1.0 OD1 A:ASP498 3.0 79.7 1.0 OD1 A:ASP151 3.0 80.5 1.0 OD2 A:ASP437 3.2 80.4 1.0 CG A:ASP437 3.3 81.5 1.0 MG A:MG601 3.5 89.0 1.0 CB A:ASP498 4.2 76.4 1.0 OD1 A:ASP94 4.3 83.6 1.0 CB A:ASP151 4.4 76.0 1.0 O A:HOH703 4.4 77.0 1.0 O A:ASP499 4.4 77.1 1.0 N A:GLY438 4.6 74.0 1.0 NZ A:LYS88 4.7 81.6 1.0 CB A:ASP437 4.8 76.9 1.0 N A:ASP499 4.9 74.8 1.0

Magnesium binding site 3 out of 4 in the Structure of Wild-Type PPM1H Phosphatase at 3.1 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structure of Wild-Type PPM1H Phosphatase at 3.1 Angstrom Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg601 b:91.9 occ:1.00 OD2 B:ASP498 2.2 95.0 1.0 OD2 B:ASP151 2.4 87.9 1.0 OD1 B:ASP437 2.7 92.0 1.0 OD1 B:ASP151 2.9 103.8 1.0 O B:HOH701 2.9 92.7 1.0 CG B:ASP151 3.0 93.5 1.0 CG B:ASP498 3.1 96.2 1.0 OD2 B:ASP437 3.2 93.1 1.0 MG B:MG602 3.3 95.2 1.0 CG B:ASP437 3.3 93.7 1.0 OD1 B:ASP498 3.3 98.3 1.0 NZ B:LYS88 4.4 101.3 1.0 CB B:ASP498 4.4 98.3 1.0 CB B:ASP151 4.5 87.3 1.0 O B:HOH704 4.7 83.9 1.0 CB B:ASP437 4.8 90.7 1.0 N B:GLY438 4.9 87.3 1.0

Magnesium binding site 4 out of 4 in the Structure of Wild-Type PPM1H Phosphatase at 3.1 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Structure of Wild-Type PPM1H Phosphatase at 3.1 Angstrom Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg602 b:95.2 occ:1.00 OD1 B:ASP151 2.3 103.8 1.0 O B:GLY152 2.6 98.2 1.0 MG B:MG601 3.3 91.9 1.0 CG B:ASP151 3.5 93.5 1.0 OD2 B:ASP499 3.5 102.9 1.0 OD1 B:ASP498 3.6 98.3 1.0 C B:GLY152 3.8 97.5 1.0 OD1 B:ASP94 3.9 100.0 1.0 OD2 B:ASP151 4.0 87.9 1.0 N B:GLY152 4.1 89.6 1.0 CB B:GLU93 4.2 100.8 1.0 OE1 B:GLU93 4.3 105.1 1.0 O B:HOH701 4.3 92.7 1.0 OD2 B:ASP498 4.4 95.0 1.0 CG B:ASP498 4.4 96.2 1.0 C B:ASP151 4.5 91.9 1.0 CA B:GLY152 4.5 91.0 1.0 CG B:ASP499 4.6 102.2 1.0 CB B:ASP151 4.7 87.3 1.0 CA B:ASP151 4.7 89.0 1.0 C B:GLU93 4.7 101.6 1.0 CB B:ASP499 4.8 101.5 1.0 NZ B:LYS88 4.8 101.3 1.0 O B:GLU93 4.8 103.2 1.0 N B:HIS153 4.9 95.0 1.0 CE B:LYS88 4.9 99.1 1.0 CA B:GLU93 5.0 103.6 1.0 CG B:ASP94 5.0 100.4 1.0

A.R.Khan, D.Waschbusch. Structure of Wild-Type PPM1H Phosphatase at 3.1 Angstrom Resolution To Be Published.