Magnesium in PDB 2qvr: E. Coli Fructose-1,6-Bisphosphatase: Citrate, Fru-2,6-P2, and MG2+ Bound

All present enzymatic activity of E. Coli Fructose-1,6-Bisphosphatase: Citrate, Fru-2,6-P2, and MG2+ Bound:
3.1.3.11;

The structure of E. Coli Fructose-1,6-Bisphosphatase: Citrate, Fru-2,6-P2, and MG2+ Bound, PDB code: 2qvr was solved by J.K.Hines, H.J.Fromm, R.B.Honzatko, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.44 / 2.18
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	44.002, 82.251, 174.194, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 24.2

The binding sites of Magnesium atom in the E. Coli Fructose-1,6-Bisphosphatase: Citrate, Fru-2,6-P2, and MG2+ Bound (pdb code 2qvr). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the E. Coli Fructose-1,6-Bisphosphatase: Citrate, Fru-2,6-P2, and MG2+ Bound, PDB code: 2qvr:

Magnesium binding site 1 out of 1 in the E. Coli Fructose-1,6-Bisphosphatase: Citrate, Fru-2,6-P2, and MG2+ Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of E. Coli Fructose-1,6-Bisphosphatase: Citrate, Fru-2,6-P2, and MG2+ Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg334 b:32.7 occ:0.50 OD1 A:ASP110 2.1 28.7 1.0 OD1 A:ASP113 2.2 38.3 1.0 OE1 A:GLU275 2.3 34.0 1.0 O1 A:FDP333 2.4 33.6 1.0 O A:HOH462 2.5 42.1 1.0 CG A:ASP110 3.0 27.6 1.0 CG A:ASP113 3.1 34.0 1.0 CB A:ASP113 3.2 31.2 1.0 CA A:ASP113 3.3 29.6 1.0 OD2 A:ASP110 3.3 25.8 1.0 CD A:GLU275 3.4 30.5 1.0 C1 A:FDP333 3.8 28.0 1.0 CG A:GLU275 3.8 29.6 1.0 O3 A:FDP333 4.0 23.3 1.0 OE2 A:GLU89 4.1 40.4 1.0 OE1 A:GLU89 4.1 43.7 1.0 N A:GLY114 4.2 30.0 1.0 C A:ASP113 4.3 30.4 1.0 OD2 A:ASP113 4.3 34.4 1.0 N A:ASP113 4.3 29.6 1.0 O2P A:FDP333 4.4 39.5 1.0 CB A:ASP110 4.4 25.3 1.0 OE2 A:GLU275 4.4 32.5 1.0 CD A:GLU89 4.5 41.0 1.0 O A:LEU112 4.5 28.5 1.0 C3 A:FDP333 4.6 27.1 1.0 C2 A:FDP333 4.6 29.3 1.0 O A:HOH404 4.7 39.8 1.0 CD1 A:ILE127 4.8 22.2 1.0 C A:LEU112 4.8 29.3 1.0 O2 A:FDP333 5.0 29.9 1.0

J.K.Hines, X.Chen, J.C.Nix, H.J.Fromm, R.B.Honzatko. Structures of Mammalian and Bacterial Fructose-1,6-Bisphosphatase Reveal the Basis For Synergism in Amp/Fructose 2,6-Bisphosphate Inhibition. J.Biol.Chem. V. 282 36121 2007.
ISSN: ISSN 0021-9258
PubMed: 17933867
DOI: 10.1074/JBC.M707302200