Magnesium in PDB 4gx6: Amp Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation E192Q

All present enzymatic activity of Amp Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation E192Q:
3.1.3.11;

The structure of Amp Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation E192Q, PDB code: 4gx6 was solved by Y.Gao, R.B.Honzatko, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.56 / 2.50
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	59.923, 165.341, 79.112, 90.00, 90.00, 90.00
R / Rfree (%)	21.1 / 27.3

The binding sites of Magnesium atom in the Amp Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation E192Q (pdb code 4gx6). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Amp Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation E192Q, PDB code: 4gx6:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Amp Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation E192Q


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Amp Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation E192Q within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:10.8 occ:1.00 O2 A:PO4405 1.9 45.3 1.0 OD2 A:ASP121 2.0 20.8 1.0 OD2 A:ASP118 2.0 27.8 1.0 OE2 A:GLU280 2.0 24.5 1.0 O1 A:F6P401 2.4 25.4 1.0 P A:PO4405 2.8 47.2 1.0 OE1 A:GLU97 3.0 31.9 1.0 CG A:ASP121 3.1 25.1 1.0 CD A:GLU280 3.2 24.8 1.0 O4 A:PO4405 3.2 49.1 1.0 CG A:ASP118 3.2 23.3 1.0 O3 A:PO4405 3.4 44.9 1.0 C1 A:F6P401 3.7 22.1 1.0 CB A:ASP121 3.7 23.1 1.0 CG A:GLU280 3.8 24.8 1.0 OD1 A:ASP118 3.9 22.5 1.0 CD A:GLU97 3.9 29.9 1.0 CA A:ASP121 4.0 22.8 1.0 MG A:MG403 4.1 19.5 1.0 O1 A:PO4405 4.1 48.9 1.0 OE2 A:GLU97 4.2 35.0 1.0 OE1 A:GLU280 4.2 28.3 1.0 OD1 A:ASP121 4.2 27.0 1.0 CB A:ASP118 4.4 21.9 1.0 O3 A:F6P401 4.6 19.6 1.0 N A:GLY122 4.7 22.8 1.0 C2 A:F6P401 4.7 24.1 1.0 O2 A:F6P401 4.9 20.2 1.0 C3 A:F6P401 4.9 21.3 1.0 C A:ASP121 4.9 22.6 1.0

Magnesium binding site 2 out of 4 in the Amp Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation E192Q


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Amp Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation E192Q within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg403 b:19.5 occ:1.00 OE2 A:GLU97 1.8 35.0 1.0 OD1 A:ASP118 2.2 22.5 1.0 O2 A:PO4405 2.4 45.3 1.0 O1 A:PO4405 2.5 48.9 1.0 O A:LEU120 2.6 21.0 1.0 CD A:GLU97 2.9 29.9 1.0 P A:PO4405 3.0 47.2 1.0 CG A:ASP118 3.1 23.3 1.0 OD2 A:ASP118 3.4 27.8 1.0 C A:LEU120 3.4 21.9 1.0 OE1 A:GLU97 3.4 31.9 1.0 OE1 A:GLU98 3.6 45.9 1.0 O A:HOH590 3.6 36.5 1.0 N A:LEU120 3.9 22.1 1.0 MG A:MG402 4.1 10.8 1.0 O4 A:PO4405 4.1 49.1 1.0 OE2 A:GLU98 4.1 42.8 1.0 N A:ASP121 4.1 22.9 1.0 CG A:GLU97 4.1 24.8 1.0 CA A:ASP121 4.2 22.8 1.0 O3 A:PO4405 4.2 44.9 1.0 CA A:LEU120 4.2 22.1 1.0 CD A:GLU98 4.3 40.5 1.0 CB A:GLU97 4.4 24.8 1.0 CB A:ASP118 4.4 21.9 1.0 C A:ASP118 4.5 21.3 1.0 O A:ASP118 4.6 20.5 1.0 CD A:PRO119 4.7 20.6 1.0 CA A:ASP118 4.7 21.7 1.0 N A:PRO119 4.7 21.2 1.0 CB A:LEU120 4.8 22.7 1.0 CB A:ASP121 5.0 23.1 1.0

Magnesium binding site 3 out of 4 in the Amp Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation E192Q


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Amp Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation E192Q within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg402 b:5.4 occ:1.00 OD2 B:ASP121 1.9 10.8 1.0 OD2 B:ASP118 2.0 25.7 1.0 OE2 B:GLU280 2.0 25.7 1.0 O3 B:PO4405 2.3 43.5 1.0 O4 B:PO4405 2.4 39.5 1.0 OE1 B:GLU97 2.5 33.4 1.0 O1 B:F6P401 2.6 27.7 1.0 P B:PO4405 2.7 42.3 1.0 CD B:GLU280 2.9 25.2 1.0 CG B:ASP121 3.0 18.5 1.0 CG B:ASP118 3.1 22.8 1.0 O2 B:PO4405 3.3 40.3 1.0 CB B:ASP121 3.5 19.8 1.0 OD1 B:ASP118 3.5 28.7 1.0 OE1 B:GLU280 3.6 26.7 1.0 CD B:GLU97 3.6 31.1 1.0 CG B:GLU280 3.8 22.6 1.0 C1 B:F6P401 3.9 20.9 1.0 MG B:MG403 3.9 9.6 1.0 CA B:ASP121 4.0 20.3 1.0 OE2 B:GLU97 4.1 35.1 1.0 OD1 B:ASP121 4.1 20.2 1.0 O B:HOH551 4.1 38.7 1.0 O1 B:PO4405 4.1 41.9 1.0 CB B:ASP118 4.4 20.9 1.0 O B:HOH571 4.5 36.6 1.0 N B:GLY122 4.7 22.5 1.0 O3 B:F6P401 4.8 11.7 1.0 CG B:GLU97 4.9 28.6 1.0 C2 B:F6P401 4.9 21.1 1.0 CB B:GLU280 5.0 21.6 1.0 C B:ASP121 5.0 21.0 1.0

Magnesium binding site 4 out of 4 in the Amp Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation E192Q


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Amp Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation E192Q within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg403 b:9.6 occ:1.00 O4 B:PO4405 1.9 39.5 1.0 OD1 B:ASP118 2.3 28.7 1.0 O B:LEU120 2.5 22.3 1.0 OE2 B:GLU97 2.5 35.1 1.0 CD B:GLU97 3.2 31.1 1.0 P B:PO4405 3.3 42.3 1.0 C B:LEU120 3.3 21.0 1.0 CG B:ASP118 3.3 22.8 1.0 OE1 B:GLU98 3.4 37.0 1.0 O B:HOH547 3.4 55.7 1.0 OE1 B:GLU97 3.5 33.4 1.0 O1 B:PO4405 3.5 41.9 1.0 OD2 B:ASP118 3.7 25.7 1.0 CA B:ASP121 3.9 20.3 1.0 MG B:MG402 3.9 5.4 1.0 N B:LEU120 3.9 20.3 1.0 N B:ASP121 4.0 20.8 1.0 OD2 B:ASP74 4.0 44.5 1.0 O3 B:PO4405 4.1 43.5 1.0 CA B:LEU120 4.2 20.9 1.0 CD B:PRO119 4.2 18.7 1.0 O2 B:PO4405 4.4 40.3 1.0 CG B:GLU97 4.4 28.6 1.0 OD1 B:ASP74 4.5 45.3 1.0 CB B:ASP121 4.5 19.8 1.0 CD B:GLU98 4.6 37.2 1.0 CB B:ASP118 4.6 20.9 1.0 N B:PRO119 4.6 19.8 1.0 CB B:GLU97 4.6 27.7 1.0 CG B:ASP74 4.7 41.6 1.0 CB B:LEU120 4.8 20.8 1.0 C B:ASP118 4.9 19.8 1.0 OD2 B:ASP121 4.9 10.8 1.0 CA B:ASP118 4.9 20.5 1.0

Y.Gao, R.B.Honzatko. Dimer-Dimer Interface in Porcine Liver Fructose-1,6-Bisphosphatase Is Essential in Cooperative Binding of Amp To Be Published.