Magnesium in PDB 6upc: Structure of Trehalose-6-Phosphate Phosphatase From Salmonella Typhimurium in Complex with Trehalose 6-Sulfate

All present enzymatic activity of Structure of Trehalose-6-Phosphate Phosphatase From Salmonella Typhimurium in Complex with Trehalose 6-Sulfate:
3.1.3.12;

The structure of Structure of Trehalose-6-Phosphate Phosphatase From Salmonella Typhimurium in Complex with Trehalose 6-Sulfate, PDB code: 6upc was solved by K.H.O'toole, C.M.Harvey, K.N.Allen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.27 / 2.51
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	46.525, 52.639, 107.053, 90.00, 99.23, 90.00
R / Rfree (%)	19.3 / 22.8

The binding sites of Magnesium atom in the Structure of Trehalose-6-Phosphate Phosphatase From Salmonella Typhimurium in Complex with Trehalose 6-Sulfate (pdb code 6upc). 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 Trehalose-6-Phosphate Phosphatase From Salmonella Typhimurium in Complex with Trehalose 6-Sulfate, PDB code: 6upc:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of Trehalose-6-Phosphate Phosphatase From Salmonella Typhimurium in Complex with Trehalose 6-Sulfate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Trehalose-6-Phosphate Phosphatase From Salmonella Typhimurium in Complex with Trehalose 6-Sulfate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:32.4 occ:1.00 OD1 A:ASP198 2.0 37.7 1.0 O26 A:T6S302 2.0 38.2 1.0 O A:ASP22 2.0 29.4 1.0 O A:HOH434 2.2 25.6 1.0 O A:HOH413 2.2 24.8 1.0 OD2 A:ASP20 2.2 25.8 1.0 CG A:ASP198 3.0 27.4 1.0 CG A:ASP20 3.1 30.8 1.0 C A:ASP22 3.2 29.8 1.0 OD1 A:ASP20 3.4 33.6 1.0 OD2 A:ASP198 3.4 27.8 1.0 S24 A:T6S302 3.4 35.8 1.0 O27 A:T6S302 4.0 32.3 1.0 CA A:ASP22 4.1 24.6 1.0 OD2 A:ASP202 4.1 33.5 1.0 N A:ASP22 4.1 21.2 1.0 CB A:ASP199 4.2 32.1 1.0 N A:GLY23 4.2 26.2 1.0 CB A:ASP22 4.2 30.6 1.0 O25 A:T6S302 4.3 29.2 1.0 OG1 A:THR24 4.3 27.3 1.0 CB A:ASP198 4.3 28.9 1.0 CA A:GLY23 4.4 28.3 1.0 O11 A:T6S302 4.4 37.1 1.0 CB A:ASP20 4.5 31.5 1.0 N A:ASP199 4.5 31.2 1.0 N A:ASP198 4.6 24.2 1.0 C A:LEU21 4.7 27.6 1.0 C A:GLY23 4.7 25.4 1.0 N A:THR24 4.8 28.0 1.0 CA A:ASP198 4.8 31.9 1.0 C A:ASP198 4.9 35.9 1.0 N A:LEU21 4.9 26.9 1.0 C09 A:T6S302 5.0 32.1 1.0 O A:LEU21 5.0 29.1 1.0

Magnesium binding site 2 out of 2 in the Structure of Trehalose-6-Phosphate Phosphatase From Salmonella Typhimurium in Complex with Trehalose 6-Sulfate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Trehalose-6-Phosphate Phosphatase From Salmonella Typhimurium in Complex with Trehalose 6-Sulfate within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg301 b:58.5 occ:1.00 OD1 B:ASP198 2.0 62.9 1.0 O27 B:T6S302 2.1 71.2 1.0 OD2 B:ASP20 2.1 62.8 1.0 O B:ASP22 2.3 60.2 1.0 CG B:ASP20 3.1 58.4 1.0 CG B:ASP198 3.2 59.1 1.0 S24 B:T6S302 3.5 58.1 1.0 C B:ASP22 3.5 53.1 1.0 OD1 B:ASP20 3.5 60.7 1.0 OD2 B:ASP198 3.7 58.1 1.0 OD2 B:ASP202 3.7 58.1 1.0 CB B:ASP199 3.9 58.0 1.0 O26 B:T6S302 3.9 60.8 1.0 O25 B:T6S302 4.2 62.0 1.0 CA B:ASP22 4.3 54.5 1.0 N B:ASP199 4.3 61.6 1.0 CB B:ASP22 4.3 63.3 1.0 N B:ASP22 4.4 54.1 1.0 CB B:ASP198 4.4 56.5 1.0 CB B:ASP20 4.5 53.7 1.0 N B:ASP198 4.5 54.9 1.0 N B:GLY23 4.5 52.5 1.0 O11 B:T6S302 4.5 71.1 1.0 C09 B:T6S302 4.6 66.9 1.0 CG B:ASP202 4.6 52.6 1.0 CA B:GLY23 4.7 50.4 1.0 OD1 B:ASP202 4.7 48.3 1.0 OG1 B:THR24 4.7 54.1 1.0 C B:ASP198 4.8 63.8 1.0 CA B:ASP198 4.8 60.0 1.0 CA B:ASP199 4.8 59.3 1.0 OD2 B:ASP199 4.9 60.0 1.0 NZ B:LYS175 4.9 50.2 1.0 CG B:ASP199 4.9 62.4 1.0 C B:LEU21 5.0 55.0 1.0

C.M.Harvey, K.H.O'toole, C.Liu, P.Mariano, D.Dunaway-Mariano, K.N.Allen. Structural Analysis of Binding Determinants Ofsalmonella Typhimuriumtrehalose-6-Phosphate Phosphatase Using Ground-State Complexes. Biochemistry V. 59 3247 2020.
ISSN: ISSN 0006-2960
PubMed: 32786412
DOI: 10.1021/ACS.BIOCHEM.0C00317