Magnesium in PDB 1q9d: Fructose-1,6-Bisphosphatase Complexed with A New Allosteric Site Inhibitor (I-State)

All present enzymatic activity of Fructose-1,6-Bisphosphatase Complexed with A New Allosteric Site Inhibitor (I-State):
3.1.3.11;

The structure of Fructose-1,6-Bisphosphatase Complexed with A New Allosteric Site Inhibitor (I-State), PDB code: 1q9d was solved by R.B.Honzatko, J.Y.Choe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.35
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	58.860, 166.250, 80.270, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 24.6

The binding sites of Magnesium atom in the Fructose-1,6-Bisphosphatase Complexed with A New Allosteric Site Inhibitor (I-State) (pdb code 1q9d). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Fructose-1,6-Bisphosphatase Complexed with A New Allosteric Site Inhibitor (I-State), PDB code: 1q9d:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Fructose-1,6-Bisphosphatase Complexed with A New Allosteric Site Inhibitor (I-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 Complexed with A New Allosteric Site Inhibitor (I-State) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg404 b:18.2 occ:1.00 OE1 A:GLU280 2.1 21.1 1.0 OD2 A:ASP121 2.1 28.2 1.0 O1 A:PO4403 2.1 43.6 1.0 OD2 A:ASP118 2.2 31.4 1.0 CG A:ASP121 3.0 27.2 1.0 CD A:GLU280 3.1 20.6 1.0 CG A:ASP118 3.2 24.3 1.0 CB A:ASP121 3.2 24.2 1.0 P A:PO4403 3.2 45.9 1.0 O3 A:PO4403 3.5 42.9 1.0 O4 A:PO4403 3.6 44.6 1.0 CG A:GLU280 3.6 19.9 1.0 CA A:ASP121 3.6 21.2 1.0 OD1 A:ASP118 3.7 22.1 1.0 OE2 A:GLU97 3.9 35.8 1.0 C1 A:F6P401 4.0 23.6 1.0 OE2 A:GLU280 4.1 20.7 1.0 OD1 A:ASP121 4.2 26.1 1.0 CB A:ASP118 4.3 23.4 1.0 O3 A:F6P401 4.3 19.6 1.0 MG A:MG405 4.5 28.6 1.0 O2 A:PO4403 4.5 44.6 1.0 CD A:GLU97 4.5 31.9 1.0 N A:GLY122 4.5 19.8 1.0 OE1 A:GLU97 4.5 32.3 1.0 O A:HOH634 4.5 37.9 1.0 O1 A:F6P401 4.6 22.9 1.0 C A:ASP121 4.6 20.7 1.0 N A:ASP121 4.6 21.3 1.0 CD1 A:ILE135 4.7 21.1 1.0 O A:LEU120 4.7 21.3 1.0 C2 A:F6P401 4.7 23.9 1.0 O2 A:F6P401 4.7 22.2 1.0 C3 A:F6P401 4.9 23.9 1.0

Magnesium binding site 2 out of 4 in the Fructose-1,6-Bisphosphatase Complexed with A New Allosteric Site Inhibitor (I-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 Complexed with A New Allosteric Site Inhibitor (I-State) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg405 b:28.6 occ:1.00 O4 A:PO4403 2.1 44.6 1.0 OD1 A:ASP118 2.2 22.1 1.0 OE2 A:GLU97 2.3 35.8 1.0 O A:LEU120 2.4 21.3 1.0 OE1 A:GLU98 2.8 36.0 1.0 CG A:ASP118 3.2 24.3 1.0 C A:LEU120 3.3 20.2 1.0 CD A:GLU97 3.5 31.9 1.0 P A:PO4403 3.5 45.9 1.0 OD2 A:ASP118 3.6 31.4 1.0 N A:LEU120 3.9 18.4 1.0 O1 A:PO4403 3.9 43.6 1.0 CD A:GLU98 4.1 33.3 1.0 CA A:LEU120 4.1 20.0 1.0 N A:ASP121 4.2 21.3 1.0 O2 A:PO4403 4.2 44.6 1.0 CB A:GLU97 4.2 27.2 1.0 CG A:GLU97 4.3 29.7 1.0 OE1 A:GLU97 4.3 32.3 1.0 CA A:ASP121 4.4 21.2 1.0 MG A:MG404 4.5 18.2 1.0 O3 A:PO4403 4.5 42.9 1.0 CB A:ASP118 4.5 23.4 1.0 CD A:PRO119 4.6 18.2 1.0 OG A:SER123 4.6 34.7 1.0 CB A:LEU120 4.6 21.5 1.0 CG A:PRO119 4.6 16.7 1.0 N A:PRO119 4.7 20.2 1.0 CA A:ASP118 4.8 22.3 1.0 C A:ASP118 4.8 21.5 1.0 OE2 A:GLU98 4.9 34.5 1.0

Magnesium binding site 3 out of 4 in the Fructose-1,6-Bisphosphatase Complexed with A New Allosteric Site Inhibitor (I-State)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Fructose-1,6-Bisphosphatase Complexed with A New Allosteric Site Inhibitor (I-State) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg414 b:9.7 occ:1.00 O4 B:PO4413 2.0 46.3 1.0 OD2 B:ASP118 2.1 22.9 1.0 OD2 B:ASP121 2.2 18.5 1.0 OE1 B:GLU280 2.3 17.5 1.0 P B:PO4413 2.9 48.1 1.0 CG B:ASP121 3.0 21.0 1.0 O2 B:PO4413 3.1 46.4 1.0 CB B:ASP121 3.2 21.2 1.0 CD B:GLU280 3.2 15.9 1.0 CG B:ASP118 3.3 19.7 1.0 O1 B:PO4413 3.3 45.4 1.0 CA B:ASP121 3.5 21.1 1.0 CG B:GLU280 3.6 16.8 1.0 C1 B:F6P411 3.6 29.9 1.0 OE2 B:GLU97 3.7 31.1 1.0 OD1 B:ASP118 3.8 21.0 1.0 OD1 B:ASP121 4.2 21.1 1.0 N B:GLY122 4.2 22.6 1.0 O3 B:PO4413 4.2 46.0 1.0 O1 B:F6P411 4.3 33.3 1.0 OE2 B:GLU280 4.3 16.0 1.0 C B:ASP121 4.4 21.6 1.0 CB B:ASP118 4.5 17.3 1.0 N B:ASP121 4.5 19.8 1.0 O3 B:F6P411 4.5 27.4 1.0 C2 B:F6P411 4.7 27.9 1.0 O B:LEU120 4.7 22.9 1.0 C3 B:F6P411 4.8 27.4 1.0 CD B:GLU97 4.9 27.5 1.0 C B:LEU120 5.0 21.1 1.0 O2 B:F6P411 5.0 25.8 1.0

Magnesium binding site 4 out of 4 in the Fructose-1,6-Bisphosphatase Complexed with A New Allosteric Site Inhibitor (I-State)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Fructose-1,6-Bisphosphatase Complexed with A New Allosteric Site Inhibitor (I-State) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg415 b:31.6 occ:1.00 OD1 B:ASP118 2.4 21.0 1.0 O1 B:PO4413 2.4 45.4 1.0 OE1 B:GLU98 2.4 33.8 1.0 O B:LEU120 2.6 22.9 1.0 O B:HOH752 3.0 56.7 1.0 O B:HOH780 3.4 43.0 1.0 C B:LEU120 3.5 21.1 1.0 CG B:ASP118 3.6 19.7 1.0 CD B:GLU98 3.6 31.0 1.0 N B:LEU120 3.7 21.2 1.0 OE1 B:GLU97 3.7 27.9 1.0 CD B:GLU97 3.9 27.5 1.0 P B:PO4413 3.9 48.1 1.0 CG B:PRO119 4.0 20.4 1.0 OE2 B:GLU97 4.0 31.1 1.0 CA B:LEU120 4.1 21.4 1.0 CD B:PRO119 4.2 19.8 1.0 OD2 B:ASP118 4.3 22.9 1.0 CB B:GLU97 4.3 22.6 1.0 N B:PRO119 4.4 19.6 1.0 CG B:GLU98 4.4 28.7 1.0 N B:ASP121 4.5 19.8 1.0 C B:ASP118 4.5 18.0 1.0 O4 B:PO4413 4.5 46.3 1.0 OE2 B:GLU98 4.5 30.6 1.0 O3 B:PO4413 4.6 46.0 1.0 CA B:ASP118 4.6 17.6 1.0 CG B:GLU97 4.6 28.7 1.0 CB B:LEU120 4.7 20.3 1.0 O2 B:PO4413 4.7 46.4 1.0 CB B:ASP118 4.7 17.3 1.0 C B:PRO119 4.8 20.8 1.0 CA B:ASP121 4.9 21.1 1.0 CA B:PRO119 4.9 19.7 1.0 CB B:PRO119 5.0 20.2 1.0

J.Y.Choe, S.W.Nelson, K.L.Arienti, F.U.Axe, T.L.Collins, T.K.Jones, R.D.Kimmich, M.J.Newman, K.Norvell, W.C.Ripka, S.J.Romano, K.M.Short, D.H.Slee, H.J.Fromm, R.B.Honzatko. Inhibition of Fructose-1,6-Bisphosphatase By A New Class of Allosteric Effectors J.Biol.Chem. V. 278 51176 2003.
ISSN: ISSN 0021-9258
PubMed: 14530289
DOI: 10.1074/JBC.M308396200