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

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

All present enzymatic activity of Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase with Blocked 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 Blocked Subunit Pair Rotation, PDB code: 4gwy 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) 37.09 / 3.00
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 53.261, 82.571, 168.885, 90.00, 90.00, 90.00
R / Rfree (%) 21.4 / 26.6

Magnesium Binding Sites:

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

Magnesium binding site 1 out of 3 in 4gwy

Go back to Magnesium Binding Sites List in 4gwy
Magnesium binding site 1 out of 3 in the Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase with Blocked 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 Blocked Subunit Pair Rotation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg403

b:2.0
occ:1.00
 O2 A:PO4402 1.9 42.1 1.0
OD2 A:ASP118 2.0 38.7 1.0
O A:LEU120 2.2 43.5 1.0
OE1 A:GLU97 2.4 48.7 1.0
OE2 A:GLU97 2.6 49.0 1.0
CD A:GLU97 2.6 48.0 1.0
C A:LEU120 3.0 43.0 1.0
P A:PO4402 3.1 44.3 1.0
CG A:ASP118 3.1 38.8 1.0
O4 A:PO4402 3.3 42.8 1.0
OD2 A:ASP74 3.5 53.1 1.0
N A:LEU120 3.6 41.5 1.0
OD1 A:ASP118 3.6 36.5 1.0
CA A:LEU120 3.8 42.4 1.0
OE2 A:GLU98 3.9 58.9 1.0
CG A:GLU97 3.9 48.3 1.0
O3 A:PO4402 3.9 43.3 1.0
N A:ASP121 3.9 43.5 1.0
MG A:MG405 4.1 42.0 1.0
CB A:GLU97 4.2 47.6 1.0
O1 A:PO4402 4.2 41.3 1.0
CA A:ASP121 4.2 44.1 1.0
CB A:LEU120 4.2 42.1 1.0
MG A:MG404 4.3 5.3 1.0
CB A:ASP118 4.4 38.9 1.0
N A:PRO119 4.6 39.2 1.0
C A:ASP118 4.6 39.0 1.0
CA A:ASP118 4.6 39.0 1.0
CD A:PRO119 4.7 39.1 1.0
CG A:ASP74 4.8 51.9 1.0
CD A:GLU98 4.8 57.5 1.0
C A:PRO119 4.8 40.2 1.0
CG A:PRO119 4.9 39.1 1.0

Magnesium binding site 2 out of 3 in 4gwy

Go back to Magnesium Binding Sites List in 4gwy
Magnesium binding site 2 out of 3 in the Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase with Blocked 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 Blocked Subunit Pair Rotation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg404

b:5.3
occ:1.00
 OD1 A:ASP118 2.1 36.5 1.0
OE1 A:GLU280 2.2 25.5 1.0
O2 A:PO4402 2.7 42.1 1.0
O3 A:PO4402 2.9 43.3 1.0
CB A:ASP121 2.9 44.0 1.0
OD1 A:ASP121 3.0 43.5 1.0
P A:PO4402 3.1 44.3 1.0
C1 A:F6P401 3.1 43.4 1.0
CA A:ASP121 3.2 44.1 1.0
CG A:ASP118 3.2 38.8 1.0
OE2 A:GLU97 3.3 49.0 1.0
O1 A:PO4402 3.3 41.3 1.0
CD A:GLU280 3.3 28.7 1.0
CG A:ASP121 3.4 44.1 1.0
O1 A:F6P401 3.6 49.1 1.0
OD2 A:ASP118 3.7 38.7 1.0
CG A:GLU280 3.9 30.8 1.0
N A:GLY122 4.0 44.5 1.0
C A:ASP121 4.1 44.4 1.0
C2 A:F6P401 4.2 40.0 1.0
O3 A:F6P401 4.2 37.5 1.0
MG A:MG403 4.3 2.0 1.0
N A:ASP121 4.3 43.5 1.0
OE2 A:GLU280 4.4 28.0 1.0
O A:LEU120 4.4 43.5 1.0
O2 A:F6P401 4.4 40.1 1.0
C3 A:F6P401 4.5 39.1 1.0
CB A:ASP118 4.5 38.9 1.0
CD A:GLU97 4.5 48.0 1.0
O4 A:PO4402 4.5 42.8 1.0
OD2 A:ASP121 4.6 44.6 1.0
C A:LEU120 4.7 43.0 1.0
NH2 A:ARG276 4.9 47.6 1.0

Magnesium binding site 3 out of 3 in 4gwy

Go back to Magnesium Binding Sites List in 4gwy
Magnesium binding site 3 out of 3 in the Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase with Blocked 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 Blocked Subunit Pair Rotation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg405

b:42.0
occ:1.00
 OD2 A:ASP68 2.0 69.7 1.0
O4 A:PO4402 2.3 42.8 1.0
OE1 A:GLU97 2.4 48.7 1.0
CG A:ASP68 2.9 69.6 1.0
CB A:ASP68 3.0 69.7 1.0
CD A:GLU97 3.3 48.0 1.0
P A:PO4402 3.5 44.3 1.0
OE2 A:GLU98 3.6 58.9 1.0
O3 A:PO4402 3.8 43.3 1.0
OE2 A:GLU97 3.9 49.0 1.0
ND2 A:ASN64 4.0 74.0 1.0
MG A:MG403 4.1 2.0 1.0
OD1 A:ASP68 4.1 69.0 1.0
OE1 A:GLU98 4.2 59.4 1.0
O2 A:PO4402 4.2 42.1 1.0
CD A:GLU98 4.2 57.5 1.0
NH2 A:ARG276 4.2 47.6 1.0
CG A:GLU97 4.3 48.3 1.0
OD2 A:ASP74 4.3 53.1 1.0
CA A:ASP68 4.5 69.6 1.0
OG A:SER123 4.5 46.6 1.0
CG A:ASN64 4.7 74.7 1.0
O1 A:PO4402 4.7 41.3 1.0
CG2 A:VAL70 4.7 66.3 1.0
CG A:ASP74 4.8 51.9 1.0
OD1 A:ASP74 4.8 50.8 1.0
O A:GLN69 4.9 68.5 1.0
OD1 A:ASN64 4.9 74.1 1.0
C A:ASP68 5.0 69.3 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 16:03:52 2024

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