Magnesium in PDB 7txb: Structure of the Class II Fructose-1,6-Bisphophatase From Mycobacterium Tuberculosis Complexed with Substrate F1,6BP

All present enzymatic activity of Structure of the Class II Fructose-1,6-Bisphophatase From Mycobacterium Tuberculosis Complexed with Substrate F1,6BP:
3.1.3.11;

The structure of Structure of the Class II Fructose-1,6-Bisphophatase From Mycobacterium Tuberculosis Complexed with Substrate F1,6BP, PDB code: 7txb was solved by C.Abad-Zapatero, A.I.Selezneva, H.J.Gutka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.99 / 3.71
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	117.11, 117.11, 325.917, 90, 90, 120
R / Rfree (%)	21.3 / 27.3

The binding sites of Magnesium atom in the Structure of the Class II Fructose-1,6-Bisphophatase From Mycobacterium Tuberculosis Complexed with Substrate F1,6BP (pdb code 7txb). 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 the Class II Fructose-1,6-Bisphophatase From Mycobacterium Tuberculosis Complexed with Substrate F1,6BP, PDB code: 7txb:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of the Class II Fructose-1,6-Bisphophatase From Mycobacterium Tuberculosis Complexed with Substrate F1,6BP


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Class II Fructose-1,6-Bisphophatase From Mycobacterium Tuberculosis Complexed with Substrate F1,6BP within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg403 b:75.9 occ:1.00 O2P B:FBP402 2.4 85.7 1.0 O B:ILE81 2.6 75.4 1.0 OD1 B:ASP79 2.8 85.7 1.0 OD2 B:ASP79 3.6 79.4 1.0 CG B:ASP79 3.6 80.1 1.0 P1 B:FBP402 3.7 94.3 1.0 C B:ILE81 3.7 74.0 1.0 O1 B:FBP402 3.9 91.2 1.0 CG2 B:THR84 3.9 85.1 1.0 C1 B:FBP402 4.1 88.1 1.0 CA B:ASP82 4.3 70.7 1.0 N B:ASP82 4.4 72.1 1.0 OE2 B:GLU208 4.5 105.1 1.0 O1P B:FBP402 4.6 92.4 1.0 N B:GLY83 4.6 72.9 1.0 N B:ILE81 4.7 72.5 1.0 O3P B:FBP402 4.7 89.8 1.0 CA B:ILE81 4.8 71.3 1.0 OD1 B:ASP82 4.8 71.8 1.0 OD1 B:ASP27 4.9 103.6 1.0 C B:ASP82 4.9 69.6 1.0 N B:THR84 5.0 79.7 1.0

Magnesium binding site 2 out of 2 in the Structure of the Class II Fructose-1,6-Bisphophatase From Mycobacterium Tuberculosis Complexed with Substrate F1,6BP


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of the Class II Fructose-1,6-Bisphophatase From Mycobacterium Tuberculosis Complexed with Substrate F1,6BP within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:79.5 occ:1.00 O A:ILE81 2.6 90.7 1.0 O1P A:FBP401 2.8 72.0 1.0 OD1 A:ASP79 3.0 84.1 1.0 OD2 A:ASP79 3.6 73.7 1.0 CG A:ASP79 3.7 74.7 1.0 CG2 A:THR84 3.7 70.7 1.0 C A:ILE81 3.7 82.6 1.0 P1 A:FBP401 4.2 80.7 1.0 CA A:ASP82 4.4 75.2 1.0 N A:ASP82 4.4 76.8 1.0 C1 A:FBP401 4.5 74.4 1.0 OE2 A:GLU208 4.6 94.7 1.0 OD1 A:ASP27 4.7 124.4 1.0 N A:GLY83 4.7 78.0 1.0 O2P A:FBP401 4.7 78.8 1.0 O1 A:FBP401 4.7 77.5 1.0 N A:ILE81 4.8 69.7 1.0 CA A:ILE81 4.8 73.3 1.0

A.I.Selezneva, L.N.M.Harding, H.J.Gutka, F.Movahedzadeh, C.Abad-Zapatero. New Structures of Class II Fructose-1,6-Bisphosphatase From Francisella Tularensis Provide A Framework For A Novel Catalytic Mechanism For the Entire Class To Be Published.