Manganese in PDB 1fbg: 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: 1fbg 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 / 3.00
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	132.000, 132.000, 67.400, 90.00, 90.00, 120.00
R / Rfree (%)	19 / n/a

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

Manganese 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 Manganese with other atoms in the Mn 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:Mn341 b:62.8 occ:1.00 OD2 A:ASP118 2.4 43.2 1.0 OE2 A:GLU280 2.5 39.7 1.0 O1P A:AHM336 2.5 71.7 1.0 OE2 A:GLU97 2.5 65.6 1.0 OD1 A:ASP121 2.5 48.8 1.0 O2P A:AHM336 2.8 95.0 1.0 P1 A:AHM336 3.0 96.6 1.0 CG A:ASP118 3.1 30.0 1.0 CD A:GLU97 3.2 65.2 1.0 CD A:GLU280 3.3 37.7 1.0 CG A:ASP121 3.3 42.7 1.0 HH12 A:ARG276 3.5 0.0 1.0 OD1 A:ASP118 3.5 25.6 1.0 CA A:ASP121 3.5 38.8 1.0 C1 A:AHM336 3.5 85.8 1.0 CB A:ASP121 3.5 42.7 1.0 OE1 A:GLU97 3.6 73.0 1.0 O1 A:AHM336 3.6 94.5 1.0 NH1 A:ARG276 3.9 69.2 1.0 HH11 A:ARG276 3.9 0.0 1.0 CG A:GLU97 4.0 54.2 1.0 CG A:GLU280 4.1 38.4 1.0 O A:LEU120 4.1 25.7 1.0 H A:GLY122 4.1 0.0 1.0 OE1 A:GLU280 4.2 43.1 1.0 CB A:ASP118 4.3 14.9 1.0 HO3 A:AHM336 4.3 0.0 1.0 N A:ASP121 4.3 31.5 1.0 O3P A:AHM336 4.5 93.9 1.0 OD2 A:ASP121 4.5 46.7 1.0 C A:LEU120 4.5 27.2 1.0 HOP3 A:AHM336 4.6 0.0 1.0 C A:ASP121 4.6 46.2 1.0 HH22 A:ARG276 4.7 0.0 1.0 N A:GLY122 4.8 53.6 1.0 CZ A:ARG276 4.8 72.3 1.0 C2 A:AHM336 4.9 78.8 1.0 H A:ASP121 4.9 0.0 1.0

Manganese 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 Manganese with other atoms in the Mn 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:Mn341 b:78.8 occ:1.00 OE2 B:GLU280 2.4 80.2 1.0 OD2 B:ASP118 2.5 74.3 1.0 OE2 B:GLU97 2.5 77.3 1.0 O1P B:AHM336 2.6 93.7 1.0 OD1 B:ASP121 2.6 70.9 1.0 O2P B:AHM336 2.7 0.6 1.0 P1 B:AHM336 2.8 0.8 1.0 O1 B:AHM336 3.0 94.8 1.0 CD B:GLU97 3.1 71.4 1.0 CG B:ASP118 3.3 66.8 1.0 OE1 B:GLU97 3.3 67.2 1.0 CD B:GLU280 3.3 76.2 1.0 CG B:ASP121 3.5 61.8 1.0 OE1 B:GLU280 3.7 75.8 1.0 CA B:ASP121 3.8 48.3 1.0 CB B:ASP121 3.8 56.5 1.0 HO3 B:AHM336 4.0 0.0 1.0 H B:GLY122 4.0 0.0 1.0 OD1 B:ASP118 4.1 71.7 1.0 CB B:ASP118 4.1 53.8 1.0 C1 B:AHM336 4.2 63.9 1.0 CG B:GLU97 4.2 63.7 1.0 O3P B:AHM336 4.4 0.1 1.0 N B:ASP121 4.6 37.5 1.0 CG B:GLU280 4.7 72.7 1.0 HOP3 B:AHM336 4.7 0.0 1.0 N B:GLY122 4.8 55.4 1.0 OD2 B:ASP121 4.8 50.4 1.0 C B:ASP121 4.8 50.5 1.0 CB B:GLU97 4.9 62.5 1.0 O B:LEU120 5.0 36.2 1.0 C B:LEU120 5.0 32.9 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