Magnesium in PDB 4gws: Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase with Filled Central Cavity

All present enzymatic activity of Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase with Filled Central Cavity:
3.1.3.11;

The structure of Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase with Filled Central Cavity, PDB code: 4gws 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)	31.19 / 2.75
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	60.236, 164.285, 79.136, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 26.2

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

Magnesium binding site 1 out of 2 in the Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase with Filled Central Cavity


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase with Filled Central Cavity within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:20.4 occ:1.00 OE1 A:GLU280 1.9 21.5 1.0 OD2 A:ASP121 2.0 11.6 1.0 O2 A:PO4404 2.2 42.0 1.0 OD2 A:ASP118 2.3 20.0 1.0 O1 A:F6P401 2.7 20.9 1.0 O3 A:PO4404 2.8 37.8 1.0 CG A:ASP121 2.9 18.2 1.0 CD A:GLU280 3.0 18.1 1.0 P A:PO4404 3.1 38.6 1.0 CB A:ASP121 3.1 18.8 1.0 CG A:ASP118 3.4 17.8 1.0 CG A:GLU280 3.6 16.2 1.0 CA A:ASP121 3.6 19.2 1.0 O1 A:PO4404 3.8 34.4 1.0 O3 A:F6P401 3.9 14.5 1.0 OD1 A:ASP118 3.9 18.4 1.0 C1 A:F6P401 4.0 18.0 1.0 OE2 A:GLU280 4.0 17.4 1.0 OD1 A:ASP121 4.1 20.2 1.0 OE2 A:GLU97 4.2 30.0 1.0 O4 A:PO4404 4.3 38.9 1.0 N A:GLY122 4.3 22.0 1.0 O2 A:F6P401 4.4 17.7 1.0 C A:ASP121 4.5 20.6 1.0 C3 A:F6P401 4.5 17.1 1.0 C2 A:F6P401 4.5 18.8 1.0 CB A:ASP118 4.6 16.3 1.0 N A:ASP121 4.7 19.1 1.0 CD A:GLU97 4.8 28.1 1.0 OE1 A:GLU97 4.8 31.8 1.0 CD1 A:ILE135 4.8 10.6 1.0 O A:LEU120 4.9 20.2 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase with Filled Central Cavity


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase with Filled Central Cavity within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg402 b:19.9 occ:1.00 OD2 B:ASP121 1.8 9.8 1.0 OE2 B:GLU280 2.1 20.3 1.0 OD2 B:ASP118 2.2 17.6 1.0 O3 B:PO4404 2.3 42.6 1.0 O4 B:PO4404 2.3 45.7 1.0 CG B:ASP121 2.8 16.4 1.0 P B:PO4404 2.8 44.2 1.0 O1 B:F6P401 2.8 23.6 1.0 OE1 B:GLU97 3.1 27.0 1.0 CD B:GLU280 3.2 17.7 1.0 CB B:ASP121 3.2 15.6 1.0 CG B:ASP118 3.2 13.6 1.0 O2 B:PO4404 3.4 41.5 1.0 CG B:GLU280 3.7 15.3 1.0 CA B:ASP121 3.7 15.1 1.0 OD1 B:ASP118 3.8 16.4 1.0 OD1 B:ASP121 3.9 19.9 1.0 C1 B:F6P401 4.1 18.0 1.0 O1 B:PO4404 4.2 43.3 1.0 OE1 B:GLU280 4.3 18.5 1.0 CD B:GLU97 4.3 26.1 1.0 CB B:ASP118 4.3 12.1 1.0 O B:HOH515 4.4 9.7 1.0 O3 B:F6P401 4.4 13.8 1.0 O B:HOH556 4.5 29.8 1.0 N B:GLY122 4.5 17.8 1.0 C B:ASP121 4.7 16.2 1.0 N B:ASP121 4.7 14.6 1.0 C3 B:F6P401 4.8 16.6 1.0 CD1 B:ILE135 4.8 6.1 1.0 C2 B:F6P401 4.8 17.4 1.0 OE2 B:GLU97 5.0 29.0 1.0

Y.Gao, L.Shen, R.B.Honzatko. Hydrophobic Central Cavity in Fructose-1,6-Bisphosphatase Is Essential For the Synergism in Amp/Fructose 2,6-Bisphosphate Inhibition To Be Published.