Magnesium in PDB 2i33: The Structure of the Class C Acid Phosphatase From Bacillus Anthracis

All present enzymatic activity of The Structure of the Class C Acid Phosphatase From Bacillus Anthracis:
3.1.3.2;

The structure of The Structure of the Class C Acid Phosphatase From Bacillus Anthracis, PDB code: 2i33 was solved by R.L.Felts, J.J.Tanner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.12 / 1.57
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	52.231, 89.909, 104.238, 90.00, 90.00, 90.00
R / Rfree (%)	17.3 / 20.7

The binding sites of Magnesium atom in the The Structure of the Class C Acid Phosphatase From Bacillus Anthracis (pdb code 2i33). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the The Structure of the Class C Acid Phosphatase From Bacillus Anthracis, PDB code: 2i33:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the The Structure of the Class C Acid Phosphatase From Bacillus Anthracis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Structure of the Class C Acid Phosphatase From Bacillus Anthracis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg602 b:13.3 occ:1.00 O A:HOH762 1.8 26.0 1.0 OD2 A:ASP65 2.1 38.2 1.0 O A:HOH761 2.1 19.8 1.0 O A:ASP67 2.1 28.0 1.0 OD1 A:ASP180 2.2 30.7 1.0 O A:HOH763 2.2 29.7 1.0 CG A:ASP65 3.0 32.9 1.0 CG A:ASP180 3.0 28.7 1.0 OD1 A:ASP65 3.3 33.6 1.0 OD2 A:ASP180 3.3 31.6 1.0 C A:ASP67 3.3 27.8 1.0 O A:HOH652 3.9 28.7 1.0 OD2 A:ASP184 4.1 28.6 1.0 CA A:ASP67 4.1 27.7 1.0 N A:ASP67 4.1 27.7 1.0 OH A:TYR219 4.2 32.2 1.0 OG1 A:THR69 4.2 27.2 1.0 CB A:ASP67 4.2 28.5 1.0 CB A:ASP65 4.3 28.6 1.0 O A:HOH766 4.3 24.6 1.0 CB A:GLU68 4.3 27.6 1.0 N A:GLU68 4.4 27.1 1.0 O A:HOH765 4.4 23.3 1.0 CB A:ASP180 4.5 27.5 1.0 O A:HOH764 4.5 20.0 1.0 CA A:GLU68 4.6 27.3 1.0 C A:GLU68 4.7 27.3 1.0 N A:ASP180 4.8 26.8 1.0 OD1 A:ASP184 4.8 29.4 1.0 N A:THR69 4.8 26.4 1.0 CG A:ASP184 4.9 26.7 1.0 C A:LEU66 4.9 28.2 1.0 CB A:ASN181 4.9 28.2 1.0

Magnesium binding site 2 out of 2 in the The Structure of the Class C Acid Phosphatase From Bacillus Anthracis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The Structure of the Class C Acid Phosphatase From Bacillus Anthracis within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg601 b:14.8 occ:1.00 O B:HOH726 2.1 25.2 1.0 O B:ASP67 2.1 27.2 1.0 O B:HOH724 2.1 21.2 1.0 OD2 B:ASP65 2.1 32.1 1.0 O B:HOH725 2.2 19.5 1.0 OD1 B:ASP180 2.2 28.0 1.0 CG B:ASP65 2.9 30.5 1.0 CG B:ASP180 3.1 30.3 1.0 OD1 B:ASP65 3.1 31.5 1.0 C B:ASP67 3.3 28.1 1.0 OD2 B:ASP180 3.4 31.2 1.0 O B:HOH665 4.0 30.6 1.0 CA B:ASP67 4.0 27.3 1.0 N B:ASP67 4.0 27.7 1.0 OD2 B:ASP184 4.1 28.3 1.0 CB B:ASP67 4.1 27.9 1.0 OG1 B:THR69 4.2 28.7 1.0 CB B:ASP65 4.2 29.6 1.0 O B:HOH729 4.2 26.7 1.0 N B:GLU68 4.3 27.6 1.0 CB B:GLU68 4.4 28.8 1.0 OH B:TYR219 4.4 30.3 1.0 CB B:ASP180 4.5 28.0 1.0 O B:HOH728 4.5 27.4 1.0 O B:HOH727 4.5 25.6 1.0 CA B:GLU68 4.6 27.6 1.0 C B:GLU68 4.7 28.1 1.0 N B:ASP180 4.7 27.6 1.0 N B:THR69 4.7 27.8 1.0 C B:LEU66 4.8 27.3 1.0 OD1 B:ASP184 4.9 28.7 1.0 CG B:ASP184 4.9 28.4 1.0 CB B:ASN181 4.9 27.9 1.0

R.L.Felts, J.J.Tanner. The Crystal Structure of the Class C Acid Phosphatase From Bacillus Anthracis To Be Published.