Magnesium in PDB 1fbf: Crystallographic Studies of the Catalytic Mechanism of the Neutral Form of Fructose-1,6-Bisphosphatase

All present enzymatic activity of Crystallographic Studies of the Catalytic Mechanism of the Neutral Form of Fructose-1,6-Bisphosphatase:
3.1.3.11;

The structure of Crystallographic Studies of the Catalytic Mechanism of the Neutral Form of Fructose-1,6-Bisphosphatase, PDB code: 1fbf was solved by Y.Zhang, J.-Y.Liang, S.Huang, H.Ke, W.N.Lipscomb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	N/A / 2.70
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	131.400, 131.400, 69.200, 90.00, 90.00, 120.00
R / Rfree (%)	18.9 / n/a

The binding sites of Magnesium atom in the Crystallographic Studies of the Catalytic Mechanism of the Neutral Form of Fructose-1,6-Bisphosphatase (pdb code 1fbf). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystallographic Studies of the Catalytic Mechanism of the Neutral Form of Fructose-1,6-Bisphosphatase, PDB code: 1fbf:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystallographic Studies of the Catalytic Mechanism of the Neutral Form of Fructose-1,6-Bisphosphatase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystallographic Studies of the Catalytic Mechanism of the Neutral Form of Fructose-1,6-Bisphosphatase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg341 b:38.2 occ:1.00 OD2 A:ASP118 2.5 38.3 1.0 OD1 A:ASP121 2.5 36.2 1.0 OE1 A:GLU280 2.5 35.2 1.0 OE1 A:GLU97 2.5 47.5 1.0 O1P A:AHM336 2.6 54.5 1.0 CG A:ASP118 3.2 28.6 1.0 CG A:ASP121 3.3 32.9 1.0 CD A:GLU97 3.4 47.9 1.0 CD A:GLU280 3.4 19.0 1.0 OE2 A:GLU280 3.6 18.2 1.0 P1 A:AHM336 3.7 68.2 1.0 H A:GLY122 3.7 0.0 1.0 O1 A:AHM336 3.8 63.1 1.0 OD1 A:ASP118 3.9 39.2 1.0 CB A:ASP121 4.0 31.9 1.0 CB A:ASP118 4.0 22.7 1.0 CA A:ASP121 4.1 25.8 1.0 C1 A:AHM336 4.1 54.0 1.0 OD2 A:ASP121 4.1 35.7 1.0 CG A:GLU97 4.1 45.5 1.0 OE2 A:GLU97 4.2 49.8 1.0 HH11 A:ARG276 4.3 0.0 1.0 O2P A:AHM336 4.6 70.3 1.0 N A:GLY122 4.6 31.6 1.0 CG A:GLU280 4.7 19.4 1.0 NH1 A:ARG276 4.8 72.3 1.0 HH12 A:ARG276 4.8 0.0 1.0 O3P A:AHM336 4.8 67.1 1.0 CB A:GLU97 4.9 37.9 1.0 C A:ASP121 5.0 30.0 1.0 N A:ASP121 5.0 21.7 1.0

Magnesium binding site 2 out of 2 in the Crystallographic Studies of the Catalytic Mechanism of the Neutral Form of Fructose-1,6-Bisphosphatase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystallographic Studies of the Catalytic Mechanism of the Neutral Form of Fructose-1,6-Bisphosphatase within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg341 b:47.8 occ:1.00 OE2 B:GLU280 2.4 46.9 1.0 OE2 B:GLU97 2.5 52.2 1.0 OD2 B:ASP118 2.5 45.9 1.0 OD1 B:ASP121 2.6 49.3 1.0 O1P B:AHM336 2.6 59.0 1.0 CD B:GLU280 3.2 40.4 1.0 CD B:GLU97 3.3 50.3 1.0 CG B:ASP118 3.3 33.0 1.0 CG B:ASP121 3.4 40.7 1.0 CB B:ASP121 3.7 30.4 1.0 CG B:GLU280 3.8 30.9 1.0 OD1 B:ASP118 3.8 36.5 1.0 H B:GLY122 3.8 0.0 1.0 P1 B:AHM336 3.8 66.6 1.0 CA B:ASP121 3.9 25.8 1.0 O1 B:AHM336 4.0 57.0 1.0 CG B:GLU97 4.0 44.3 1.0 OE1 B:GLU280 4.1 45.9 1.0 C1 B:AHM336 4.1 39.8 1.0 OE1 B:GLU97 4.2 56.8 1.0 CB B:ASP118 4.5 27.4 1.0 OD2 B:ASP121 4.6 44.3 1.0 N B:GLY122 4.7 32.9 1.0 O3P B:AHM336 4.8 68.4 1.0 O2P B:AHM336 4.9 69.0 1.0 C B:ASP121 4.9 29.0 1.0 N B:ASP121 4.9 15.8 1.0

Y.Zhang, J.Y.Liang, S.Huang, H.Ke, W.N.Lipscomb. Crystallographic Studies of the Catalytic Mechanism of the Neutral Form of Fructose-1,6-Bisphosphatase. Biochemistry V. 32 1844 1993.
ISSN: ISSN 0006-2960
PubMed: 8382525
DOI: 10.1021/BI00058A019