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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

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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

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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

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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: Wed Aug 14 03:11:31 2024

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