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

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

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy