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Magnesium in PDB 4gx3: Product Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation R22M Reveal A T-State Conformation

Enzymatic activity of Product Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation R22M Reveal A T-State Conformation

All present enzymatic activity of Product Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation R22M Reveal A T-State Conformation:
3.1.3.11;

Protein crystallography data

The structure of Product Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation R22M Reveal A T-State Conformation, PDB code: 4gx3 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) 35.92 / 2.25
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 59.249, 165.012, 79.135, 90.00, 90.00, 90.00
R / Rfree (%) 21.2 / 27

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Product Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation R22M Reveal A T-State Conformation (pdb code 4gx3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Product Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation R22M Reveal A T-State Conformation, PDB code: 4gx3:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 4gx3

Go back to Magnesium Binding Sites List in 4gx3
Magnesium binding site 1 out of 4 in the Product Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation R22M Reveal A T-State Conformation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Product Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation R22M Reveal A T-State Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:39.0
occ:1.00
 OD2 A:ASP118 2.0 20.0 1.0
OD2 A:ASP121 2.1 19.7 1.0
OE2 A:GLU280 2.1 19.4 1.0
O2 A:PO4405 2.3 29.9 1.0
O4 A:PO4405 2.8 34.2 1.0
P A:PO4405 2.8 33.4 1.0
O1 A:F6P401 2.9 31.6 1.0
CG A:ASP121 3.0 25.5 1.0
OE2 A:GLU97 3.0 28.9 1.0
CG A:ASP118 3.1 17.3 1.0
CD A:GLU280 3.2 18.8 1.0
O3 A:PO4405 3.3 34.6 1.0
CB A:ASP121 3.3 20.5 1.0
OD1 A:ASP118 3.6 15.9 1.0
CA A:ASP121 3.7 19.8 1.0
CG A:GLU280 3.7 18.9 1.0
CD A:GLU97 4.1 26.9 1.0
OD1 A:ASP121 4.1 27.9 1.0
OE1 A:GLU280 4.2 21.9 1.0
O1 A:PO4405 4.3 36.0 1.0
C1 A:F6P401 4.3 26.4 1.0
CB A:ASP118 4.3 16.6 1.0
MG A:MG403 4.3 38.4 1.0
N A:GLY122 4.4 19.1 1.0
OE1 A:GLU97 4.4 36.3 1.0
O3 A:F6P401 4.5 11.5 1.0
C A:ASP121 4.6 18.9 1.0
O2 A:F6P401 4.6 17.2 1.0
N A:ASP121 4.7 18.9 1.0
O A:HOH583 4.8 43.5 1.0
O A:LEU120 4.8 19.3 1.0
O A:HOH613 4.8 34.4 1.0
C2 A:F6P401 4.8 22.5 1.0
C3 A:F6P401 4.8 19.5 1.0
CD1 A:ILE135 5.0 16.6 1.0

Magnesium binding site 2 out of 4 in 4gx3

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Magnesium binding site 2 out of 4 in the Product Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation R22M Reveal A T-State Conformation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Product Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation R22M Reveal A T-State Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg403

b:38.4
occ:1.00
 OD1 A:ASP118 2.1 15.9 1.0
O A:LEU120 2.3 19.3 1.0
O2 A:PO4405 2.5 29.9 1.0
OE2 A:GLU97 3.2 28.9 1.0
C A:LEU120 3.2 17.7 1.0
CG A:ASP118 3.2 17.3 1.0
OE1 A:GLU98 3.2 40.5 1.0
N A:LEU120 3.7 16.3 1.0
P A:PO4405 3.7 33.4 1.0
OD2 A:ASP118 3.8 20.0 1.0
CD A:GLU97 3.8 26.9 1.0
O1 A:PO4405 3.8 36.0 1.0
CD A:PRO119 3.8 14.4 1.0
CA A:LEU120 4.0 18.2 1.0
N A:ASP121 4.0 18.9 1.0
CD A:GLU98 4.1 36.4 1.0
OE2 A:GLU98 4.2 43.2 1.0
CA A:ASP121 4.2 19.8 1.0
CG A:GLU97 4.3 23.0 1.0
MG A:MG402 4.3 39.0 1.0
CB A:GLU97 4.4 19.4 1.0
N A:PRO119 4.4 15.6 1.0
CB A:ASP118 4.5 16.6 1.0
C A:ASP118 4.5 16.4 1.0
OE1 A:GLU97 4.5 36.3 1.0
CA A:ASP118 4.5 16.4 1.0
CG A:PRO119 4.6 13.1 1.0
CB A:LEU120 4.6 17.8 1.0
O4 A:PO4405 4.7 34.2 1.0
C A:PRO119 4.8 16.6 1.0
O3 A:PO4405 4.8 34.6 1.0
CB A:ASP121 5.0 20.5 1.0

Magnesium binding site 3 out of 4 in 4gx3

Go back to Magnesium Binding Sites List in 4gx3
Magnesium binding site 3 out of 4 in the Product Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation R22M Reveal A T-State Conformation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Product Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation R22M Reveal A T-State Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg402

b:28.4
occ:1.00
 OD2 B:ASP118 1.8 16.6 1.0
OD2 B:ASP121 1.9 18.6 1.0
O4 B:PO4405 2.2 30.6 1.0
OE1 B:GLU280 2.3 16.6 1.0
OE1 B:GLU97 2.4 21.6 1.0
O3 B:PO4405 2.5 26.6 1.0
P B:PO4405 2.8 26.0 1.0
O1 B:F6P401 2.9 31.4 1.0
CG B:ASP118 2.9 15.6 1.0
CG B:ASP121 3.0 20.8 1.0
CD B:GLU280 3.3 14.6 1.0
OD1 B:ASP118 3.3 15.5 1.0
CB B:ASP121 3.4 19.8 1.0
O2 B:PO4405 3.5 25.5 1.0
CD B:GLU97 3.6 21.4 1.0
CG B:GLU280 3.6 14.6 1.0
O B:HOH509 3.8 36.6 1.0
CA B:ASP121 3.9 18.6 1.0
OE2 B:GLU97 4.0 26.9 1.0
C1 B:F6P401 4.1 20.2 1.0
OD1 B:ASP121 4.1 19.1 1.0
O1 B:PO4405 4.1 30.3 1.0
CB B:ASP118 4.2 14.1 1.0
MG B:MG403 4.3 38.8 1.0
OE2 B:GLU280 4.4 16.4 1.0
O B:HOH587 4.6 29.8 1.0
N B:GLY122 4.7 20.3 1.0
O B:LEU120 4.7 22.0 1.0
CG B:GLU97 4.8 20.8 1.0
C B:ASP121 4.9 20.1 1.0
N B:ASP121 4.9 18.4 1.0
O2 B:F6P401 4.9 22.2 1.0
C2 B:F6P401 4.9 21.8 1.0

Magnesium binding site 4 out of 4 in 4gx3

Go back to Magnesium Binding Sites List in 4gx3
Magnesium binding site 4 out of 4 in the Product Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation R22M Reveal A T-State Conformation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Product Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Mutation R22M Reveal A T-State Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg403

b:38.8
occ:1.00
 O B:LEU120 2.1 22.0 1.0
OD1 B:ASP118 2.1 15.5 1.0
O4 B:PO4405 2.7 30.6 1.0
C B:LEU120 3.0 18.9 1.0
OE2 B:GLU97 3.1 26.9 1.0
CG B:ASP118 3.4 15.6 1.0
OD1 B:ASP74 3.4 40.9 1.0
N B:LEU120 3.4 17.0 1.0
OE1 B:GLU98 3.4 29.2 1.0
CD B:GLU97 3.6 21.4 1.0
CA B:LEU120 3.7 18.4 1.0
OE1 B:GLU97 3.7 21.6 1.0
OD2 B:ASP74 3.8 44.6 1.0
O1 B:PO4405 3.9 30.3 1.0
N B:ASP121 3.9 18.4 1.0
P B:PO4405 3.9 26.0 1.0
CD B:PRO119 3.9 14.6 1.0
OD2 B:ASP118 4.0 16.6 1.0
O B:HOH510 4.0 25.1 1.0
CG B:ASP74 4.0 39.5 1.0
CA B:ASP121 4.1 18.6 1.0
CB B:LEU120 4.2 18.4 1.0
N B:PRO119 4.3 15.8 1.0
MG B:MG402 4.3 28.4 1.0
CG B:PRO119 4.4 14.6 1.0
CD B:GLU98 4.4 29.0 1.0
C B:ASP118 4.5 15.2 1.0
CB B:ASP118 4.5 14.1 1.0
C B:PRO119 4.6 16.0 1.0
CA B:ASP118 4.6 14.6 1.0
CB B:GLU97 4.6 22.0 1.0
CG B:GLU97 4.7 20.8 1.0
CB B:ASP121 4.8 19.8 1.0
O3 B:PO4405 4.8 26.6 1.0
O2 B:PO4405 4.9 25.5 1.0

Reference:

Y.Gao, R.B.Honzatko. Dimer-Dimer Interface in Porcine Liver Fructose-1,6-Bisphosphatase Is Essential in Cooperative Binding of Amp To Be Published.
Page generated: Fri Aug 16 16:04:12 2024

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