Zinc in PDB 2qvv: Porcine Liver Fructose-1,6-Bisphosphatase Cocrystallized with Fru-2,6- P2 and ZN2+, I(T)-State

All present enzymatic activity of Porcine Liver Fructose-1,6-Bisphosphatase Cocrystallized with Fru-2,6- P2 and ZN2+, I(T)-State:
3.1.3.11;

The structure of Porcine Liver Fructose-1,6-Bisphosphatase Cocrystallized with Fru-2,6- P2 and ZN2+, I(T)-State, PDB code: 2qvv was solved by J.K.Hines, X.Chen, J.C.Nix, 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)	47.33 / 2.03
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	59.038, 165.709, 79.167, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 23.4

The binding sites of Zinc atom in the Porcine Liver Fructose-1,6-Bisphosphatase Cocrystallized with Fru-2,6- P2 and ZN2+, I(T)-State (pdb code 2qvv). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Porcine Liver Fructose-1,6-Bisphosphatase Cocrystallized with Fru-2,6- P2 and ZN2+, I(T)-State, PDB code: 2qvv:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Porcine Liver Fructose-1,6-Bisphosphatase Cocrystallized with Fru-2,6- P2 and ZN2+, I(T)-State


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Porcine Liver Fructose-1,6-Bisphosphatase Cocrystallized with Fru-2,6- P2 and ZN2+, I(T)-State within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn403 b:22.0 occ:1.00 OD2 A:ASP118 2.1 18.0 1.0 OE2 A:GLU280 2.2 21.4 1.0 O A:HOH613 2.2 20.4 1.0 OD2 A:ASP121 2.2 20.9 1.0 O1 A:FDP402 2.3 22.9 1.0 CG A:ASP118 3.1 20.3 1.0 CG A:ASP121 3.2 19.9 1.0 CD A:GLU280 3.2 23.5 1.0 OD1 A:ASP118 3.4 21.7 1.0 CB A:ASP121 3.4 19.0 1.0 C1 A:FDP402 3.5 18.7 1.0 CA A:ASP121 3.6 21.6 1.0 CG A:GLU280 3.7 21.7 1.0 NH1 A:ARG276 3.8 26.6 1.0 O3 A:FDP402 3.9 16.2 1.0 N A:GLY122 4.3 21.4 1.0 OD1 A:ASP121 4.3 19.9 1.0 OE1 A:GLU280 4.3 23.1 1.0 C3 A:FDP402 4.3 16.7 1.0 O A:HOH641 4.3 37.7 1.0 CB A:ASP118 4.4 20.6 1.0 C2 A:FDP402 4.4 18.9 1.0 O2P A:FDP402 4.5 23.4 1.0 C A:ASP121 4.5 22.6 1.0 N A:ASP121 4.7 23.2 1.0 CD1 A:ILE135 4.9 22.0 1.0 O2 A:FDP402 4.9 19.1 1.0 CZ A:ARG276 5.0 27.7 1.0

Zinc binding site 2 out of 2 in the Porcine Liver Fructose-1,6-Bisphosphatase Cocrystallized with Fru-2,6- P2 and ZN2+, I(T)-State


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Porcine Liver Fructose-1,6-Bisphosphatase Cocrystallized with Fru-2,6- P2 and ZN2+, I(T)-State within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn339 b:19.3 occ:1.00 OD2 B:ASP118 2.0 15.3 1.0 OE1 B:GLU280 2.1 16.2 1.0 OD2 B:ASP121 2.1 14.8 1.0 O B:HOH673 2.1 19.3 1.0 O1 B:FDP338 2.3 20.5 1.0 CG B:ASP118 3.0 17.4 1.0 CG B:ASP121 3.1 17.7 1.0 CD B:GLU280 3.1 19.9 1.0 CB B:ASP121 3.4 17.8 1.0 OD1 B:ASP118 3.5 18.9 1.0 C1 B:FDP338 3.5 19.3 1.0 CG B:GLU280 3.6 17.4 1.0 CA B:ASP121 3.6 19.6 1.0 NH2 B:ARG276 3.7 19.3 1.0 O3 B:FDP338 4.0 18.8 1.0 O B:HOH510 4.2 30.9 1.0 OD1 B:ASP121 4.2 17.4 1.0 OE2 B:GLU280 4.2 20.2 1.0 N B:GLY122 4.3 21.4 1.0 CB B:ASP118 4.3 15.4 1.0 C3 B:FDP338 4.4 18.7 1.0 O3P B:FDP338 4.4 23.0 1.0 C2 B:FDP338 4.4 18.7 1.0 C B:ASP121 4.5 20.9 1.0 N B:ASP121 4.7 20.0 1.0 CD1 B:ILE135 4.8 18.1 1.0 CG B:GLU97 4.9 24.8 1.0 CZ B:ARG276 4.9 24.1 1.0 O2 B:FDP338 5.0 19.4 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