Magnesium in PDB 1eyi: Fructose-1,6-Bisphosphatase Complex with Magnesium, Fructose-6- Phosphate and Phosphate (R-State)

All present enzymatic activity of Fructose-1,6-Bisphosphatase Complex with Magnesium, Fructose-6- Phosphate and Phosphate (R-State):
3.1.3.11;

The structure of Fructose-1,6-Bisphosphatase Complex with Magnesium, Fructose-6- Phosphate and Phosphate (R-State), PDB code: 1eyi was solved by J.Choe, R.B.Honzatko, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	5.00 / 2.32
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	52.120, 82.510, 165.490, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 24.2

The binding sites of Magnesium atom in the Fructose-1,6-Bisphosphatase Complex with Magnesium, Fructose-6- Phosphate and Phosphate (R-State) (pdb code 1eyi). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Fructose-1,6-Bisphosphatase Complex with Magnesium, Fructose-6- Phosphate and Phosphate (R-State), PDB code: 1eyi:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Fructose-1,6-Bisphosphatase Complex with Magnesium, Fructose-6- Phosphate and Phosphate (R-State)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Fructose-1,6-Bisphosphatase Complex with Magnesium, Fructose-6- Phosphate and Phosphate (R-State) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg341 b:13.8 occ:1.00 O A:LEU120 2.1 13.9 1.0 OD2 A:ASP118 2.1 17.7 1.0 O A:HOH587 2.2 14.8 1.0 OE1 A:GLU97 2.2 22.1 1.0 O2 A:PO4340 2.3 36.0 1.0 O4 A:PO4340 2.4 37.5 1.0 P A:PO4340 2.8 34.0 1.0 CG A:ASP118 3.0 16.4 1.0 C A:LEU120 3.0 15.1 1.0 OD1 A:ASP118 3.3 18.2 1.0 CD A:GLU97 3.4 24.6 1.0 CA A:ASP121 3.7 18.9 1.0 N A:ASP121 3.7 17.0 1.0 O3 A:PO4340 3.8 35.0 1.0 MG A:MG342 3.8 27.7 1.0 N A:LEU120 3.9 10.7 1.0 OE2 A:GLU97 3.9 31.5 1.0 CA A:LEU120 4.0 14.2 1.0 O1 A:PO4340 4.0 33.6 1.0 OE2 A:GLU98 4.4 21.1 1.0 CB A:ASP118 4.4 14.3 1.0 NH2 A:ARG276 4.6 39.6 1.0 O A:HOH616 4.6 40.3 1.0 OD2 A:ASP74 4.6 32.2 1.0 CB A:LEU120 4.6 16.3 1.0 CG A:GLU97 4.6 22.9 1.0 CB A:ASP121 4.7 17.9 1.0 CA A:ASP118 4.7 12.9 1.0 C A:ASP118 4.7 13.7 1.0 C A:ASP121 4.8 18.9 1.0 OG A:SER123 4.8 34.5 1.0 CB A:GLU97 4.8 19.2 1.0 CD A:PRO119 4.9 13.2 1.0 N A:PRO119 4.9 13.3 1.0 O1 A:F6P339 4.9 27.6 1.0 N A:GLY122 4.9 19.8 1.0

Magnesium binding site 2 out of 2 in the Fructose-1,6-Bisphosphatase Complex with Magnesium, Fructose-6- Phosphate and Phosphate (R-State)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Fructose-1,6-Bisphosphatase Complex with Magnesium, Fructose-6- Phosphate and Phosphate (R-State) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg342 b:27.7 occ:1.00 OD1 A:ASP121 1.9 18.6 1.0 O2 A:PO4340 2.0 36.0 1.0 OE1 A:GLU280 2.0 15.4 1.0 OD1 A:ASP118 2.2 18.2 1.0 O1 A:F6P339 2.3 27.6 1.0 CG A:ASP121 2.9 19.6 1.0 CD A:GLU280 3.2 14.8 1.0 CB A:ASP121 3.2 17.9 1.0 P A:PO4340 3.3 34.0 1.0 CG A:ASP118 3.4 16.4 1.0 CA A:ASP121 3.4 18.9 1.0 C1 A:F6P339 3.6 22.3 1.0 CG A:GLU280 3.7 14.7 1.0 O1 A:PO4340 3.7 33.6 1.0 MG A:MG341 3.8 13.8 1.0 O3 A:PO4340 3.9 35.0 1.0 OD2 A:ASP118 3.9 17.7 1.0 N A:GLY122 4.0 19.8 1.0 O3 A:F6P339 4.0 16.2 1.0 OD2 A:ASP121 4.0 20.5 1.0 NH2 A:ARG276 4.1 39.6 1.0 OE2 A:GLU280 4.2 16.0 1.0 C A:ASP121 4.3 18.9 1.0 O4 A:PO4340 4.4 37.5 1.0 OE1 A:GLU97 4.5 22.1 1.0 C3 A:F6P339 4.5 19.7 1.0 C2 A:F6P339 4.5 21.9 1.0 CB A:ASP118 4.5 14.3 1.0 N A:ASP121 4.6 17.0 1.0 O A:LEU120 4.6 13.9 1.0 CD1 A:ILE135 4.6 5.8 1.0 CE A:MET248 4.7 24.4 1.0 O2 A:F6P339 4.9 21.2 1.0 C A:LEU120 5.0 15.1 1.0

J.Y.Choe, H.J.Fromm, R.B.Honzatko. Crystal Structures of Fructose 1,6-Bisphosphatase: Mechanism of Catalysis and Allosteric Inhibition Revealed in Product Complexes. Biochemistry V. 39 8565 2000.
ISSN: ISSN 0006-2960
PubMed: 10913263
DOI: 10.1021/BI000574G