Magnesium in PDB 1eyj: Fructose-1,6-Bisphosphatase Complex with Amp, Magnesium, Fructose-6- Phosphate and Phosphate (T-State)

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

The structure of Fructose-1,6-Bisphosphatase Complex with Amp, Magnesium, Fructose-6- Phosphate and Phosphate (T-State), PDB code: 1eyj 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 / 2.28
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	59.860, 165.820, 79.510, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 25.5

The binding sites of Magnesium atom in the Fructose-1,6-Bisphosphatase Complex with Amp, Magnesium, Fructose-6- Phosphate and Phosphate (T-State) (pdb code 1eyj). 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 Amp, Magnesium, Fructose-6- Phosphate and Phosphate (T-State), PDB code: 1eyj:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Fructose-1,6-Bisphosphatase Complex with Amp, Magnesium, Fructose-6- Phosphate and Phosphate (T-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 Amp, Magnesium, Fructose-6- Phosphate and Phosphate (T-State) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg339 b:26.3 occ:1.00 OD2 A:ASP118 2.0 16.4 1.0 OE2 A:GLU280 2.1 20.1 1.0 OD2 A:ASP121 2.1 22.0 1.0 O2 A:PO4340 2.2 52.0 1.0 O1 A:F6P338 2.4 25.5 1.0 CG A:ASP121 3.1 22.2 1.0 CG A:ASP118 3.1 15.4 1.0 P A:PO4340 3.1 53.0 1.0 O4 A:PO4340 3.3 52.0 1.0 CD A:GLU280 3.3 20.2 1.0 CB A:ASP121 3.3 20.5 1.0 O3 A:PO4340 3.5 51.6 1.0 CA A:ASP121 3.6 20.0 1.0 OD1 A:ASP118 3.6 15.6 1.0 C1 A:F6P338 3.8 21.3 1.0 OE2 A:GLU97 3.8 33.3 1.0 CG A:GLU280 4.0 18.1 1.0 N A:GLY122 4.2 21.1 1.0 OE1 A:GLU280 4.2 20.4 1.0 OD1 A:ASP121 4.3 22.4 1.0 CB A:ASP118 4.3 14.5 1.0 O3 A:F6P338 4.3 16.5 1.0 O1 A:PO4340 4.4 52.5 1.0 C A:ASP121 4.5 20.1 1.0 CD A:GLU97 4.5 30.5 1.0 O A:HOH750 4.5 26.8 1.0 OE1 A:GLU97 4.6 32.2 1.0 C2 A:F6P338 4.7 20.6 1.0 C3 A:F6P338 4.7 18.8 1.0 N A:ASP121 4.7 18.3 1.0 O2 A:F6P338 4.9 21.4 1.0

Magnesium binding site 2 out of 2 in the Fructose-1,6-Bisphosphatase Complex with Amp, Magnesium, Fructose-6- Phosphate and Phosphate (T-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 Amp, Magnesium, Fructose-6- Phosphate and Phosphate (T-State) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg344 b:17.3 occ:1.00 OD2 B:ASP121 2.0 18.0 1.0 O4 B:PO4343 2.0 49.3 1.0 OD2 B:ASP118 2.1 19.3 1.0 OE1 B:GLU280 2.1 16.8 1.0 O1 B:F6P341 2.3 21.3 1.0 P B:PO4343 3.0 49.1 1.0 CG B:ASP121 3.0 20.5 1.0 O3 B:PO4343 3.0 49.1 1.0 CG B:ASP118 3.2 17.8 1.0 CD B:GLU280 3.2 16.8 1.0 OE1 B:GLU97 3.3 33.7 1.0 CB B:ASP121 3.5 18.3 1.0 O2 B:PO4343 3.7 48.4 1.0 C1 B:F6P341 3.7 18.7 1.0 CA B:ASP121 3.7 17.4 1.0 OD1 B:ASP118 3.7 18.3 1.0 CG B:GLU280 3.9 16.0 1.0 OD1 B:ASP121 4.0 23.9 1.0 O1 B:PO4343 4.2 48.9 1.0 OE2 B:GLU280 4.3 16.7 1.0 N B:GLY122 4.3 17.5 1.0 CB B:ASP118 4.4 16.9 1.0 O3 B:F6P341 4.4 15.0 1.0 O B:HOH683 4.5 34.8 1.0 CD B:GLU97 4.5 30.6 1.0 C B:ASP121 4.5 17.2 1.0 C2 B:F6P341 4.6 18.4 1.0 N B:ASP121 4.8 16.7 1.0 C3 B:F6P341 4.8 16.6 1.0 O2 B:F6P341 4.9 19.1 1.0 CD1 B:ILE135 5.0 11.7 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