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Magnesium in PDB 4gwz: Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase with Restrained Subunit Pair Rotation

Enzymatic activity of Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase with Restrained Subunit Pair Rotation

All present enzymatic activity of Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase with Restrained Subunit Pair Rotation:
3.1.3.11;

Protein crystallography data

The structure of Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase with Restrained Subunit Pair Rotation, PDB code: 4gwz was solved by Y.Gao, R.B.Honzatko, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.84 / 2.60
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 59.776, 166.064, 79.871, 90.00, 90.00, 90.00
R / Rfree (%) 21.1 / 27.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase with Restrained Subunit Pair Rotation (pdb code 4gwz). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase with Restrained Subunit Pair Rotation, PDB code: 4gwz:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 4gwz

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Magnesium binding site 1 out of 4 in the Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase with Restrained Subunit Pair Rotation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase with Restrained Subunit Pair Rotation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:37.0
occ:1.00
 OE2 A:GLU280 1.9 35.5 1.0
OD2 A:ASP118 2.0 33.0 1.0
O2 A:PO4405 2.2 55.9 1.0
OD2 A:ASP121 2.2 30.4 1.0
O4 A:PO4405 2.7 56.8 1.0
P A:PO4405 2.9 56.5 1.0
OE1 A:GLU97 3.0 44.5 1.0
O1 A:F6P401 3.0 33.1 1.0
CD A:GLU280 3.1 32.6 1.0
CG A:ASP118 3.2 28.3 1.0
CG A:ASP121 3.2 32.0 1.0
CB A:ASP121 3.5 29.3 1.0
O3 A:PO4405 3.5 55.1 1.0
CG A:GLU280 3.7 29.3 1.0
OD1 A:ASP118 3.7 27.5 1.0
CA A:ASP121 3.9 29.5 1.0
OE1 A:GLU280 4.1 31.1 1.0
MG A:MG403 4.1 37.5 1.0
CD A:GLU97 4.2 40.0 1.0
O A:HOH562 4.3 55.0 1.0
O1 A:PO4405 4.3 57.9 1.0
CB A:ASP118 4.4 27.5 1.0
C1 A:F6P401 4.4 30.9 1.0
OD1 A:ASP121 4.4 35.0 1.0
O3 A:F6P401 4.6 26.6 1.0
N A:GLY122 4.7 29.0 1.0
C A:ASP121 4.9 29.4 1.0
O2 A:F6P401 4.9 26.8 1.0
OE2 A:GLU97 4.9 41.3 1.0
N A:ASP121 5.0 29.6 1.0

Magnesium binding site 2 out of 4 in 4gwz

Go back to Magnesium Binding Sites List in 4gwz
Magnesium binding site 2 out of 4 in the Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase with Restrained Subunit Pair Rotation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase with Restrained Subunit Pair Rotation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg403

b:37.5
occ:1.00
 OD1 A:ASP118 2.2 27.5 1.0
O2 A:PO4405 2.2 55.9 1.0
O A:LEU120 2.7 30.1 1.0
OE2 A:GLU97 2.9 41.3 1.0
O1 A:PO4405 3.1 57.9 1.0
CD A:GLU97 3.1 40.0 1.0
OE1 A:GLU97 3.1 44.5 1.0
P A:PO4405 3.2 56.5 1.0
CG A:ASP118 3.3 28.3 1.0
OE1 A:GLU98 3.5 48.6 1.0
C A:LEU120 3.5 29.3 1.0
OD2 A:ASP118 3.6 33.0 1.0
OE2 A:GLU98 4.0 47.0 1.0
MG A:MG402 4.1 37.0 1.0
N A:LEU120 4.2 28.0 1.0
O4 A:PO4405 4.2 56.8 1.0
CD A:GLU98 4.2 45.9 1.0
CA A:ASP121 4.2 29.5 1.0
N A:ASP121 4.2 29.6 1.0
CG A:GLU97 4.2 37.4 1.0
CB A:GLU97 4.2 36.6 1.0
CA A:LEU120 4.4 28.8 1.0
O3 A:PO4405 4.4 55.1 1.0
CD A:PRO119 4.5 27.1 1.0
CB A:ASP118 4.6 27.5 1.0
CA A:ASP118 4.9 27.4 1.0
CB A:LEU120 4.9 28.6 1.0
CB A:ASP121 4.9 29.3 1.0
C A:ASP118 4.9 27.6 1.0
N A:PRO119 5.0 27.9 1.0

Magnesium binding site 3 out of 4 in 4gwz

Go back to Magnesium Binding Sites List in 4gwz
Magnesium binding site 3 out of 4 in the Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase with Restrained Subunit Pair Rotation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase with Restrained Subunit Pair Rotation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg402

b:54.4
occ:1.00
 O4 B:PO4405 1.8 55.1 1.0
OD2 B:ASP121 2.0 24.5 1.0
OE1 B:GLU280 2.0 33.1 1.0
OD2 B:ASP118 2.1 35.7 1.0
O3 B:PO4405 2.2 54.0 1.0
OE1 B:GLU97 2.4 37.8 1.0
P B:PO4405 2.5 53.8 1.0
CG B:ASP121 3.1 30.1 1.0
CG B:ASP118 3.2 28.3 1.0
CD B:GLU280 3.2 31.1 1.0
O2 B:PO4405 3.3 50.7 1.0
OD1 B:ASP118 3.6 29.9 1.0
CD B:GLU97 3.6 37.9 1.0
CB B:ASP121 3.7 29.8 1.0
MG B:MG403 3.8 44.8 1.0
O1 B:PO4405 3.8 53.9 1.0
C1 B:F6P401 3.8 23.7 1.0
CG B:GLU280 4.0 28.2 1.0
CA B:ASP121 4.1 30.4 1.0
OD1 B:ASP121 4.2 31.5 1.0
OE2 B:GLU280 4.2 31.8 1.0
O1 B:F6P401 4.2 26.2 1.0
OE2 B:GLU97 4.2 40.3 1.0
CB B:ASP118 4.4 25.6 1.0
O B:HOH542 4.6 33.9 1.0
CG B:GLU97 4.7 39.5 1.0
O B:LEU120 4.8 31.7 1.0
N B:GLY122 4.8 31.9 1.0
O2 B:F6P401 4.9 20.0 1.0
C2 B:F6P401 4.9 22.1 1.0
C B:ASP121 5.0 31.0 1.0

Magnesium binding site 4 out of 4 in 4gwz

Go back to Magnesium Binding Sites List in 4gwz
Magnesium binding site 4 out of 4 in the Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase with Restrained Subunit Pair Rotation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase with Restrained Subunit Pair Rotation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg403

b:44.8
occ:1.00
 OD1 B:ASP118 2.3 29.9 1.0
O4 B:PO4405 2.4 55.1 1.0
O B:LEU120 2.4 31.7 1.0
OE2 B:GLU97 3.0 40.3 1.0
O1 B:PO4405 3.2 53.9 1.0
CG B:ASP118 3.3 28.3 1.0
C B:LEU120 3.4 31.1 1.0
OE1 B:GLU97 3.4 37.8 1.0
CD B:GLU97 3.4 37.9 1.0
P B:PO4405 3.4 53.8 1.0
OE1 B:GLU98 3.4 43.6 1.0
OD2 B:ASP118 3.6 35.7 1.0
MG B:MG402 3.8 54.4 1.0
N B:LEU120 3.9 29.8 1.0
CD B:PRO119 4.1 26.6 1.0
N B:ASP121 4.2 31.1 1.0
CA B:ASP121 4.2 30.4 1.0
CA B:LEU120 4.2 30.4 1.0
O3 B:PO4405 4.3 54.0 1.0
CB B:GLU97 4.5 38.8 1.0
CG B:GLU97 4.5 39.5 1.0
CD B:GLU98 4.5 44.5 1.0
O2 B:PO4405 4.6 50.7 1.0
N B:PRO119 4.6 26.9 1.0
CB B:ASP118 4.6 25.6 1.0
CB B:LEU120 4.7 30.6 1.0
CB B:ASP121 4.8 29.8 1.0
C B:ASP118 4.8 26.2 1.0
CA B:ASP118 4.9 25.9 1.0
OD2 B:ASP121 4.9 24.5 1.0

Reference:

Y.Gao, L.Shen, R.B.Honzatko. Functional Importance of Subunit Pair Rotation in Regulation of Tetrameric Mammalian Fructose-1,6-Bisphosphatase To Be Published.
Page generated: Fri Aug 16 16:04:02 2024

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