Magnesium in PDB 2g9y: Structure of S102T E. Coli Alkaline Phosphatase in Presence of Phosphate at 2.00 A Resolution

All present enzymatic activity of Structure of S102T E. Coli Alkaline Phosphatase in Presence of Phosphate at 2.00 A Resolution:
3.1.3.1;

The structure of Structure of S102T E. Coli Alkaline Phosphatase in Presence of Phosphate at 2.00 A Resolution, PDB code: 2g9y was solved by J.Wang, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.70 / 2.00
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	76.460, 164.490, 192.530, 90.00, 90.00, 90.00
R / Rfree (%)	20.5 / 24.2

The structure of Structure of S102T E. Coli Alkaline Phosphatase in Presence of Phosphate at 2.00 A Resolution also contains other interesting chemical elements:

Zinc

(Zn)

4 atoms

The binding sites of Magnesium atom in the Structure of S102T E. Coli Alkaline Phosphatase in Presence of Phosphate at 2.00 A Resolution (pdb code 2g9y). 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 S102T E. Coli Alkaline Phosphatase in Presence of Phosphate at 2.00 A Resolution, PDB code: 2g9y:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of S102T E. Coli Alkaline Phosphatase in Presence of Phosphate at 2.00 A 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 S102T E. Coli Alkaline Phosphatase in Presence of Phosphate at 2.00 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg452 b:20.7 occ:1.00 O A:HOH804 2.1 38.9 1.0 OE2 A:GLU322 2.1 20.5 1.0 OD2 A:ASP51 2.2 19.4 1.0 O A:HOH752 2.2 37.4 1.0 O A:HOH977 2.5 46.8 1.0 OG1 A:THR155 2.6 27.7 1.0 CD A:GLU322 3.2 22.6 1.0 CG A:ASP51 3.2 19.3 1.0 OD2 A:ASP153 3.3 23.7 1.0 CB A:THR155 3.4 23.5 1.0 OE1 A:GLU322 3.6 16.8 1.0 CB A:ASP51 3.8 16.5 1.0 OG1 A:THR102 3.8 30.8 1.0 O A:HOH721 3.9 28.4 1.0 N A:THR155 4.1 20.8 1.0 OD1 A:ASP51 4.2 18.0 1.0 CB A:ALA324 4.3 22.1 1.0 CG A:ASP153 4.3 22.3 1.0 CA A:THR155 4.4 22.6 1.0 CG2 A:THR155 4.5 24.6 1.0 CG A:GLU322 4.5 20.2 1.0 CA A:ALA324 4.6 22.1 1.0 CB A:THR102 4.6 27.9 1.0 ZN A:ZN451 4.7 25.0 1.0 CG2 A:THR102 4.8 30.2 1.0 O A:ALA324 4.8 22.1 1.0 OD1 A:ASP153 4.9 23.2 1.0 OD1 A:ASP369 5.0 16.3 1.0

Magnesium binding site 2 out of 2 in the Structure of S102T E. Coli Alkaline Phosphatase in Presence of Phosphate at 2.00 A 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 S102T E. Coli Alkaline Phosphatase in Presence of Phosphate at 2.00 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg452 b:21.0 occ:1.00 OD2 B:ASP51 2.1 28.1 1.0 O B:HOH1127 2.1 27.5 1.0 OE2 B:GLU322 2.2 28.8 1.0 O B:HOH1128 2.5 28.3 1.0 OG1 B:THR155 2.5 31.4 1.0 O B:HOH1191 2.6 49.0 1.0 CG B:ASP51 3.1 23.8 1.0 CD B:GLU322 3.3 28.4 1.0 CB B:THR155 3.4 29.5 1.0 CG2 B:THR102 3.6 26.4 1.0 OD2 B:ASP153 3.6 35.2 1.0 OE1 B:GLU322 3.7 29.6 1.0 CB B:ASP51 3.8 20.8 1.0 O B:HOH1107 3.9 31.3 1.0 OD1 B:ASP51 4.0 21.9 1.0 N B:THR155 4.2 29.3 1.0 OG1 B:THR102 4.3 30.9 1.0 CA B:THR155 4.4 28.7 1.0 CB B:ALA324 4.4 26.2 1.0 CG B:ASP153 4.5 32.5 1.0 CG2 B:THR155 4.5 26.0 1.0 CB B:THR102 4.5 28.9 1.0 CG B:GLU322 4.6 27.2 1.0 ZN B:ZN451 4.6 27.1 1.0 CA B:ALA324 4.7 25.7 1.0 O B:ALA324 4.7 26.2 1.0 OD1 B:ASP369 4.9 20.4 1.0

J.Wang, E.R.Kantrowitz. Trapping the Tetrahedral Intermediate in the Alkaline Phosphatase Reaction By Substitution of the Active Site Serine with Threonine. Protein Sci. V. 15 2395 2006.
ISSN: ISSN 0961-8368
PubMed: 17008720
DOI: 10.1110/PS.062351506