Magnesium in PDB 1fbc: 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: 1fbc 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 / 2.60
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	131.400, 131.400, 68.900, 90.00, 90.00, 120.00
R / Rfree (%)	18.5 / 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 1fbc). 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: 1fbc:
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:47.7 occ:1.00 OD2 A:ASP118 2.5 43.9 1.0 O1P A:AHG336 2.6 68.2 1.0 OE2 A:GLU280 2.6 45.3 1.0 OD1 A:ASP121 2.6 43.1 1.0 OE1 A:GLU97 2.7 53.9 1.0 CD A:GLU280 3.0 28.1 1.0 O2P A:AHG336 3.0 88.9 1.0 P1 A:AHG336 3.2 86.0 1.0 OE1 A:GLU280 3.2 40.6 1.0 CG A:ASP118 3.3 34.5 1.0 CD A:GLU97 3.4 49.6 1.0 CG A:ASP121 3.4 35.6 1.0 HH11 A:ARG276 3.6 0.0 1.0 O1 A:AHG336 3.8 85.7 1.0 HH12 A:ARG276 3.9 0.0 1.0 CB A:ASP121 3.9 33.9 1.0 H A:GLY122 3.9 0.0 1.0 CA A:ASP121 3.9 29.5 1.0 CG A:GLU97 3.9 41.9 1.0 CG A:GLU280 4.0 25.4 1.0 NH1 A:ARG276 4.1 59.8 1.0 OD1 A:ASP118 4.1 39.9 1.0 CB A:ASP118 4.3 24.0 1.0 OE2 A:GLU97 4.4 49.6 1.0 OD2 A:ASP121 4.5 39.9 1.0 O3P A:AHG336 4.6 86.0 1.0 HO3 A:AHG336 4.7 0.0 1.0 HOP3 A:AHG336 4.7 0.0 1.0 N A:GLY122 4.8 35.6 1.0 N A:ASP121 4.9 25.3 1.0 C A:ASP121 4.9 33.5 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:60.2 occ:1.00 OE2 B:GLU280 2.5 51.7 1.0 OD2 B:ASP118 2.6 57.4 1.0 O1P B:AHG336 2.6 83.7 1.0 OE1 B:GLU97 2.7 64.7 1.0 OD1 B:ASP121 2.7 57.3 1.0 CD B:GLU97 3.3 59.6 1.0 CD B:GLU280 3.3 39.9 1.0 OE2 B:GLU97 3.4 67.3 1.0 CG B:ASP118 3.4 40.2 1.0 P1 B:AHG336 3.6 0.6 1.0 H B:GLY122 3.7 0.0 1.0 CG B:ASP121 3.7 52.1 1.0 O2P B:AHG336 3.8 0.7 1.0 CG B:GLU280 3.9 36.1 1.0 HO3 B:AHG336 4.0 0.0 1.0 OD1 B:ASP118 4.1 45.8 1.0 CA B:ASP121 4.1 41.3 1.0 H2 B:HOH345 4.2 0.0 1.0 OE1 B:GLU280 4.2 43.8 1.0 CB B:ASP121 4.3 47.7 1.0 CB B:ASP118 4.5 31.8 1.0 O B:HOH345 4.5 52.2 1.0 N B:GLY122 4.6 41.0 1.0 HOP3 B:AHG336 4.6 0.0 1.0 O3P B:AHG336 4.7 98.2 1.0 CG B:GLU97 4.7 52.5 1.0 OD2 B:ASP121 4.8 52.0 1.0 O1 B:AHG336 4.8 94.0 1.0 C B:ASP121 4.9 42.1 1.0 O3 B:AHG336 4.9 52.4 1.0 H1 B:HOH345 4.9 0.0 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