Atomistry » Magnesium » PDB 4gnk-4gyp » 4gwz
Atomistry »
  Magnesium »
    PDB 4gnk-4gyp »
      4gwz »

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

Go back to Magnesium Binding Sites List in 4gwz
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

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy