Magnesium in PDB 4gx4: Amp Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation R22M

All present enzymatic activity of Amp Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation R22M:
3.1.3.11;

The structure of Amp Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation R22M, PDB code: 4gx4 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)	32.24 / 2.50
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	60.776, 166.535, 79.209, 90.00, 90.00, 90.00
R / Rfree (%)	21.4 / 27.1

The binding sites of Magnesium atom in the Amp Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation R22M (pdb code 4gx4). 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 R22M, PDB code: 4gx4:
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 R22M


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 R22M within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:11.5 occ:1.00 OE2 A:GLU280 1.8 27.9 1.0 O2 A:PO4405 1.8 46.0 1.0 OD2 A:ASP121 1.9 22.1 1.0 OD2 A:ASP118 2.0 35.2 1.0 O1 A:F6P401 2.8 21.1 1.0 CG A:ASP121 2.9 27.8 1.0 CD A:GLU280 2.9 28.2 1.0 CG A:ASP118 3.2 28.5 1.0 P A:PO4405 3.2 48.0 1.0 OE1 A:GLU97 3.3 43.2 1.0 CB A:ASP121 3.4 27.5 1.0 CG A:GLU280 3.5 26.4 1.0 O1 A:PO4405 3.6 46.1 1.0 OD1 A:ASP118 3.9 29.3 1.0 O3 A:PO4405 3.9 46.6 1.0 C1 A:F6P401 3.9 17.3 1.0 OE1 A:GLU280 4.0 29.7 1.0 OD1 A:ASP121 4.0 31.4 1.0 CA A:ASP121 4.0 27.8 1.0 CD A:GLU97 4.1 38.7 1.0 OE2 A:GLU97 4.1 43.3 1.0 CB A:ASP118 4.2 24.8 1.0 MG A:MG403 4.2 23.0 1.0 O4 A:PO4405 4.3 48.1 1.0 O3 A:F6P401 4.4 18.9 1.0 N A:GLY122 4.7 27.9 1.0 C2 A:F6P401 4.8 21.8 1.0 C3 A:F6P401 4.8 19.2 1.0 CB A:GLU280 4.8 24.5 1.0 CD1 A:ILE135 4.9 24.6 1.0 C A:ASP121 4.9 27.7 1.0 O2 A:F6P401 5.0 21.0 1.0

Magnesium binding site 2 out of 4 in the Amp Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation R22M


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 R22M within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg403 b:23.0 occ:1.00 OD1 A:ASP118 1.8 29.3 1.0 O1 A:PO4405 1.9 46.1 1.0 OE2 A:GLU97 1.9 43.3 1.0 O A:LEU120 2.3 28.8 1.0 CG A:ASP118 2.7 28.5 1.0 CD A:GLU97 3.1 38.7 1.0 OD2 A:ASP118 3.1 35.2 1.0 C A:LEU120 3.2 27.2 1.0 P A:PO4405 3.3 48.0 1.0 OE1 A:GLU98 3.3 49.6 1.0 O2 A:PO4405 3.5 46.0 1.0 N A:LEU120 3.6 25.9 1.0 OE1 A:GLU97 3.8 43.2 1.0 N A:ASP121 4.0 27.9 1.0 CA A:ASP121 4.0 27.8 1.0 CA A:LEU120 4.0 26.8 1.0 OE2 A:GLU98 4.0 47.6 1.0 CB A:ASP118 4.1 24.8 1.0 C A:ASP118 4.1 23.3 1.0 CD A:GLU98 4.1 46.0 1.0 CG A:GLU97 4.1 34.6 1.0 OD1 A:ASP74 4.2 47.5 1.0 MG A:MG402 4.2 11.5 1.0 O4 A:PO4405 4.3 48.1 1.0 O3 A:PO4405 4.3 46.6 1.0 O A:ASP118 4.3 21.7 1.0 CA A:ASP118 4.3 24.3 1.0 N A:PRO119 4.4 23.8 1.0 CD A:PRO119 4.4 23.6 1.0 CB A:GLU97 4.4 32.9 1.0 CB A:ASP121 4.6 27.5 1.0 CB A:LEU120 4.7 25.8 1.0 OD2 A:ASP74 4.8 48.2 1.0 C A:PRO119 4.8 25.8 1.0 CG A:PRO119 4.8 22.2 1.0 CG A:ASP74 4.9 45.0 1.0

Magnesium binding site 3 out of 4 in the Amp Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation R22M


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 R22M within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg402 b:5.6 occ:1.00 OD1 B:ASP121 1.8 25.5 1.0 OE1 B:GLU280 1.8 22.1 1.0 OD2 B:ASP118 1.9 35.1 1.0 O3 B:PO4405 2.0 39.3 1.0 OE1 B:GLU97 2.2 36.4 1.0 O4 B:PO4405 2.2 35.0 1.0 P B:PO4405 2.6 40.6 1.0 O1 B:F6P401 2.7 25.6 1.0 CG B:ASP121 3.0 23.7 1.0 CD B:GLU280 3.0 23.0 1.0 CG B:ASP118 3.1 30.0 1.0 CD B:GLU97 3.4 35.6 1.0 O2 B:PO4405 3.5 32.3 1.0 OD1 B:ASP118 3.7 35.9 1.0 CG B:GLU280 3.8 20.8 1.0 OD2 B:ASP121 3.8 11.5 1.0 MG B:MG403 3.9 10.0 1.0 O1 B:PO4405 3.9 42.4 1.0 OE2 B:GLU97 4.0 38.1 1.0 OE2 B:GLU280 4.0 23.0 1.0 CB B:ASP121 4.0 24.4 1.0 C1 B:F6P401 4.1 19.8 1.0 O B:HOH578 4.1 47.0 1.0 CA B:ASP121 4.2 24.9 1.0 CB B:ASP118 4.3 24.7 1.0 CG B:GLU97 4.6 31.5 1.0 O B:LEU120 4.8 23.7 1.0 N B:GLY122 4.9 27.3 1.0 O3 B:F6P401 5.0 14.2 1.0 C2 B:F6P401 5.0 21.9 1.0

Magnesium binding site 4 out of 4 in the Amp Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation R22M


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 R22M within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg403 b:10.0 occ:1.00 O4 B:PO4405 2.0 35.0 1.0 OD1 B:ASP118 2.2 35.9 1.0 O B:LEU120 2.3 23.7 1.0 OE2 B:GLU97 2.6 38.1 1.0 O1 B:PO4405 2.9 42.4 1.0 P B:PO4405 3.0 40.6 1.0 CD B:GLU97 3.1 35.6 1.0 CG B:ASP118 3.2 30.0 1.0 OE1 B:GLU97 3.3 36.4 1.0 C B:LEU120 3.3 24.1 1.0 O B:HOH562 3.5 48.1 1.0 OD2 B:ASP118 3.5 35.1 1.0 OE1 B:GLU98 3.6 40.3 1.0 MG B:MG402 3.9 5.6 1.0 O3 B:PO4405 3.9 39.3 1.0 N B:LEU120 4.0 24.2 1.0 OD1 B:ASP74 4.1 48.4 1.0 N B:ASP121 4.2 24.7 1.0 CA B:ASP121 4.2 24.9 1.0 CA B:LEU120 4.2 24.0 1.0 O2 B:PO4405 4.3 32.3 1.0 CG B:GLU97 4.3 31.5 1.0 CB B:GLU97 4.4 30.6 1.0 OD1 B:ASP121 4.5 25.5 1.0 CD B:PRO119 4.5 23.2 1.0 CB B:ASP118 4.6 24.7 1.0 N B:PRO119 4.7 23.6 1.0 CB B:LEU120 4.7 24.2 1.0 CD B:GLU98 4.7 40.5 1.0 CA B:ASP118 4.9 24.1 1.0 OD2 B:ASP74 4.9 49.9 1.0 C B:ASP118 5.0 23.7 1.0 CG B:ASP74 5.0 45.8 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.