Atomistry » Magnesium » PDB 2qrn-2r1y » 2qvu
Atomistry »
  Magnesium »
    PDB 2qrn-2r1y »
      2qvu »

Magnesium in PDB 2qvu: Porcine Liver Fructose-1,6-Bisphosphatase Cocrystallized with Fru-2,6- P2 and MG2+, I(T)-State

Enzymatic activity of Porcine Liver Fructose-1,6-Bisphosphatase Cocrystallized with Fru-2,6- P2 and MG2+, I(T)-State

All present enzymatic activity of Porcine Liver Fructose-1,6-Bisphosphatase Cocrystallized with Fru-2,6- P2 and MG2+, I(T)-State:
3.1.3.11;

Protein crystallography data

The structure of Porcine Liver Fructose-1,6-Bisphosphatase Cocrystallized with Fru-2,6- P2 and MG2+, I(T)-State, PDB code: 2qvu 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) 48.15 / 1.50
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 59.173, 165.627, 79.618, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 21.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Porcine Liver Fructose-1,6-Bisphosphatase Cocrystallized with Fru-2,6- P2 and MG2+, I(T)-State (pdb code 2qvu). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Porcine Liver Fructose-1,6-Bisphosphatase Cocrystallized with Fru-2,6- P2 and MG2+, I(T)-State, PDB code: 2qvu:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 2qvu

Go back to Magnesium Binding Sites List in 2qvu
Magnesium binding site 1 out of 4 in the Porcine Liver Fructose-1,6-Bisphosphatase Cocrystallized with Fru-2,6- P2 and MG2+, I(T)-State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Porcine Liver Fructose-1,6-Bisphosphatase Cocrystallized with Fru-2,6- P2 and MG2+, I(T)-State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg340

b:11.8
occ:1.00
OE2 A:GLU280 2.0 13.3 1.0
O A:HOH700 2.0 15.8 1.0
OD2 A:ASP118 2.0 13.2 1.0
OD2 A:ASP121 2.0 10.8 1.0
O1 A:FDP338 2.1 12.6 1.0
CG A:ASP118 3.0 13.1 1.0
CG A:ASP121 3.1 11.6 1.0
CD A:GLU280 3.1 13.4 1.0
C1 A:FDP338 3.3 11.7 1.0
OD1 A:ASP118 3.4 14.7 1.0
CB A:ASP121 3.5 11.9 1.0
NH1 A:ARG276 3.7 17.3 1.0
CA A:ASP121 3.7 13.5 1.0
CG A:GLU280 3.8 12.7 1.0
O3 A:FDP338 3.9 10.0 1.0
OE1 A:GLU280 4.1 12.7 1.0
OD1 A:ASP121 4.2 11.5 1.0
O2P A:FDP338 4.2 14.0 1.0
C3 A:FDP338 4.3 9.8 1.0
N A:GLY122 4.3 14.7 1.0
C2 A:FDP338 4.3 11.8 1.0
O A:HOH438 4.4 15.8 1.0
CB A:ASP118 4.4 13.4 1.0
C A:ASP121 4.5 13.9 1.0
N A:ASP121 4.8 14.1 1.0
CG A:GLU97 4.8 16.8 1.0
O2 A:FDP338 4.9 11.0 1.0
CZ A:ARG276 4.9 18.0 1.0
OE1 A:GLU97 5.0 20.6 1.0
CD1 A:ILE135 5.0 10.9 1.0
CD A:GLU97 5.0 18.2 1.0

Magnesium binding site 2 out of 4 in 2qvu

Go back to Magnesium Binding Sites List in 2qvu
Magnesium binding site 2 out of 4 in the Porcine Liver Fructose-1,6-Bisphosphatase Cocrystallized with Fru-2,6- P2 and MG2+, I(T)-State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Porcine Liver Fructose-1,6-Bisphosphatase Cocrystallized with Fru-2,6- P2 and MG2+, I(T)-State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg341

b:20.4
occ:1.00
O A:HOH389 2.1 23.9 1.0
OE1 A:GLU97 2.1 20.6 1.0
O A:HOH613 2.1 25.4 1.0
O A:HOH438 2.1 15.8 1.0
O A:HOH459 2.2 19.4 1.0
O A:HOH574 2.2 22.8 1.0
CD A:GLU97 3.2 18.2 1.0
OE2 A:GLU97 3.5 18.8 1.0
O A:HOH677 4.1 26.1 1.0
NH1 A:ARG276 4.1 17.3 1.0
O A:HOH852 4.1 40.6 1.0
O A:HOH700 4.2 15.8 1.0
O2P A:FDP338 4.2 14.0 1.0
O A:HOH441 4.3 18.5 1.0
O A:HOH687 4.4 27.6 1.0
NH2 A:ARG276 4.4 18.3 1.0
O A:HOH648 4.4 23.0 1.0
CG A:GLU97 4.5 16.8 1.0
CB A:SER123 4.6 14.1 1.0
O1P A:FDP338 4.6 15.3 1.0
O A:HOH853 4.7 48.9 1.0
CZ A:ARG276 4.7 18.0 1.0
O1 A:FDP338 4.9 12.6 1.0
O A:HOH656 5.0 22.7 1.0

Magnesium binding site 3 out of 4 in 2qvu

Go back to Magnesium Binding Sites List in 2qvu
Magnesium binding site 3 out of 4 in the Porcine Liver Fructose-1,6-Bisphosphatase Cocrystallized with Fru-2,6- P2 and MG2+, I(T)-State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Porcine Liver Fructose-1,6-Bisphosphatase Cocrystallized with Fru-2,6- P2 and MG2+, I(T)-State within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg344

b:11.0
occ:1.00
OE1 B:GLU280 1.9 11.1 1.0
OD2 B:ASP121 2.0 10.2 1.0
OD2 B:ASP118 2.0 13.4 1.0
O B:HOH600 2.0 14.6 1.0
O1 B:FDP339 2.1 10.9 1.0
CG B:ASP121 3.1 10.8 1.0
CG B:ASP118 3.1 12.9 1.0
CD B:GLU280 3.1 13.7 1.0
C1 B:FDP339 3.3 10.7 1.0
OD1 B:ASP118 3.5 14.0 1.0
CB B:ASP121 3.5 12.2 1.0
NH2 B:ARG276 3.6 16.8 1.0
CG B:GLU280 3.7 12.9 1.0
CA B:ASP121 3.7 13.3 1.0
O3 B:FDP339 3.9 10.8 1.0
OE2 B:GLU280 4.1 14.0 1.0
OD1 B:ASP121 4.1 11.0 1.0
O3P B:FDP339 4.2 14.2 1.0
C3 B:FDP339 4.2 10.1 1.0
C2 B:FDP339 4.2 11.7 1.0
N B:GLY122 4.3 15.0 1.0
O B:HOH390 4.4 15.4 1.0
CB B:ASP118 4.4 12.7 1.0
C B:ASP121 4.5 13.6 1.0
CG B:GLU97 4.7 15.3 1.0
N B:ASP121 4.8 12.3 1.0
CZ B:ARG276 4.8 18.2 1.0
O2 B:FDP339 4.8 11.6 1.0
CD1 B:ILE135 4.9 11.8 1.0
CD B:GLU97 4.9 17.0 1.0
OE2 B:GLU97 5.0 18.0 1.0

Magnesium binding site 4 out of 4 in 2qvu

Go back to Magnesium Binding Sites List in 2qvu
Magnesium binding site 4 out of 4 in the Porcine Liver Fructose-1,6-Bisphosphatase Cocrystallized with Fru-2,6- P2 and MG2+, I(T)-State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Porcine Liver Fructose-1,6-Bisphosphatase Cocrystallized with Fru-2,6- P2 and MG2+, I(T)-State within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg345

b:21.1
occ:1.00
O B:HOH390 2.1 15.4 1.0
O B:HOH596 2.1 27.1 1.0
O B:HOH622 2.1 25.3 1.0
O B:HOH566 2.2 22.3 1.0
OE2 B:GLU97 2.2 18.0 1.0
O B:HOH471 2.2 20.6 1.0
CD B:GLU97 3.2 17.0 1.0
OE1 B:GLU97 3.5 18.5 1.0
O B:HOH679 4.1 24.0 1.0
O B:HOH863 4.1 33.4 1.0
O B:HOH600 4.1 14.6 1.0
NH2 B:ARG276 4.1 16.8 1.0
O3P B:FDP339 4.2 14.2 1.0
O B:HOH410 4.2 17.1 1.0
O B:HOH499 4.3 21.5 1.0
NH1 B:ARG276 4.4 17.7 1.0
O B:HOH643 4.5 21.4 1.0
CG B:GLU97 4.5 15.3 1.0
CB B:SER123 4.6 13.9 1.0
O1P B:FDP339 4.6 15.5 1.0
OE1 B:GLU98 4.7 34.7 1.0
CZ B:ARG276 4.8 18.2 1.0
O1 B:FDP339 4.9 10.9 1.0
O B:HOH515 4.9 25.6 1.0

Reference:

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
Page generated: Sun Aug 10 13:38:16 2025

Last articles

Mn in 9LJU
Mn in 9LJW
Mn in 9LJS
Mn in 9LJR
Mn in 9LJT
Mn in 9LJV
Mg in 9UA2
Mg in 9R96
Mg in 9VM1
Mg in 9P01
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy