Magnesium in PDB 2ga3: Structure of S102T E. Coli Alkaline Phosphatase-Phosphate Intermediate at 2.20A Resolution

All present enzymatic activity of Structure of S102T E. Coli Alkaline Phosphatase-Phosphate Intermediate at 2.20A Resolution:
3.1.3.1;

The structure of Structure of S102T E. Coli Alkaline Phosphatase-Phosphate Intermediate at 2.20A Resolution, PDB code: 2ga3 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)	14.98 / 2.20
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	76.230, 164.970, 192.900, 90.00, 90.00, 90.00
R / Rfree (%)	19.2 / 22.9

The structure of Structure of S102T E. Coli Alkaline Phosphatase-Phosphate Intermediate at 2.20A 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-Phosphate Intermediate at 2.20A Resolution (pdb code 2ga3). 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-Phosphate Intermediate at 2.20A Resolution, PDB code: 2ga3:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of S102T E. Coli Alkaline Phosphatase-Phosphate Intermediate at 2.20A 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-Phosphate Intermediate at 2.20A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg452 b:30.2 occ:1.00 OE2 A:GLU322 2.0 25.8 1.0 O A:HOH460 2.2 23.5 1.0 O A:HOH461 2.2 31.6 1.0 OD1 A:ASP51 2.2 38.2 1.0 O A:HOH459 2.5 38.1 1.0 CD A:GLU322 3.0 25.3 1.0 OG1 A:THR155 3.2 28.0 1.0 OE1 A:GLU322 3.2 24.1 1.0 CG A:ASP51 3.3 33.0 1.0 CB A:THR155 3.6 27.4 1.0 OD2 A:ASP153 3.7 29.6 1.0 CG2 A:TPO102 3.8 26.4 1.0 CB A:ASP51 4.1 26.5 1.0 N A:THR155 4.1 25.4 1.0 OD2 A:ASP51 4.1 32.7 1.0 CB A:ALA324 4.2 30.6 1.0 O A:HOH564 4.3 41.2 1.0 CG A:GLU322 4.3 24.6 1.0 CG A:ASP153 4.5 28.8 1.0 CA A:THR155 4.5 26.3 1.0 O2P A:TPO102 4.6 34.2 1.0 CA A:ALA324 4.6 31.1 1.0 OG1 A:TPO102 4.7 30.5 1.0 CB A:TPO102 4.8 27.4 1.0 CG2 A:THR155 4.8 27.1 1.0 CD A:PRO156 4.9 27.0 1.0 O A:ALA324 5.0 32.0 1.0

Magnesium binding site 2 out of 2 in the Structure of S102T E. Coli Alkaline Phosphatase-Phosphate Intermediate at 2.20A 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-Phosphate Intermediate at 2.20A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg452 b:36.1 occ:1.00 OE2 B:GLU322 2.1 29.1 1.0 OD2 B:ASP51 2.1 38.4 1.0 O B:HOH961 2.2 40.5 1.0 O B:HOH959 2.3 35.1 1.0 O B:HOH960 2.3 41.8 1.0 OG1 B:THR155 2.9 31.8 1.0 CD B:GLU322 3.1 30.7 1.0 CG B:ASP51 3.2 32.8 1.0 OE1 B:GLU322 3.4 29.6 1.0 CB B:THR155 3.5 31.2 1.0 CG2 B:TPO102 3.8 29.1 1.0 CB B:ASP51 3.9 28.3 1.0 N B:THR155 4.2 33.2 1.0 OD1 B:ASP51 4.2 33.8 1.0 O B:HOH1094 4.2 41.9 1.0 CB B:ALA324 4.2 32.2 1.0 CG B:GLU322 4.4 29.1 1.0 CA B:THR155 4.5 32.4 1.0 OG1 B:TPO102 4.5 34.8 1.0 OD1 B:ASP153 4.6 45.0 1.0 CA B:ALA324 4.6 33.6 1.0 CG2 B:THR155 4.6 28.4 1.0 CG B:ASP153 4.7 41.5 1.0 CB B:TPO102 4.7 31.2 1.0 O1P B:TPO102 4.7 40.3 1.0 OD2 B:ASP153 4.9 42.8 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