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Magnesium in PDB 4gwu: Crystal Structure of Fru 2,6-Bisphosphate Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Filled Central Cavity

Enzymatic activity of Crystal Structure of Fru 2,6-Bisphosphate Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Filled Central Cavity

All present enzymatic activity of Crystal Structure of Fru 2,6-Bisphosphate Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Filled Central Cavity:
3.1.3.11;

Protein crystallography data

The structure of Crystal Structure of Fru 2,6-Bisphosphate Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Filled Central Cavity, PDB code: 4gwu 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) 38.54 / 3.00
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 53.999, 81.221, 165.058, 90.00, 90.00, 90.00
R / Rfree (%) 23.1 / 28.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Fru 2,6-Bisphosphate Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Filled Central Cavity (pdb code 4gwu). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Fru 2,6-Bisphosphate Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Filled Central Cavity, PDB code: 4gwu:

Magnesium binding site 1 out of 1 in 4gwu

Go back to Magnesium Binding Sites List in 4gwu
Magnesium binding site 1 out of 1 in the Crystal Structure of Fru 2,6-Bisphosphate Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Filled Central Cavity


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 Fru 2,6-Bisphosphate Complexes of Porcine Liver Fructose-1,6-Bisphosphatase with Filled Central Cavity within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:40.4
occ:1.00
 OD2 A:ASP118 2.2 50.0 1.0
O1 A:FDP401 2.3 49.2 1.0
OD1 A:ASP121 2.5 58.2 1.0
OE1 A:GLU280 2.7 43.5 1.0
OD1 A:ASP118 2.9 52.1 1.0
CG A:ASP118 2.9 51.0 1.0
OE2 A:GLU97 3.0 63.4 1.0
C1 A:FDP401 3.4 46.9 1.0
O1P A:FDP401 3.4 48.9 1.0
CG A:ASP121 3.5 55.9 1.0
CA A:ASP121 3.6 54.5 1.0
CD A:GLU97 3.8 62.5 1.0
O A:HOH526 3.8 39.5 1.0
CD A:GLU280 3.8 45.5 1.0
CB A:ASP121 3.9 54.3 1.0
NH1 A:ARG276 3.9 64.6 1.0
N A:GLY122 4.0 53.0 1.0
O A:LEU120 4.1 54.1 1.0
O2 A:FDP401 4.2 48.9 1.0
CG A:GLU97 4.3 63.0 1.0
C A:ASP121 4.3 54.2 1.0
C2 A:FDP401 4.4 47.2 1.0
CB A:ASP118 4.4 49.9 1.0
P1 A:FDP401 4.5 50.7 1.0
OE1 A:GLU97 4.5 62.4 1.0
N A:ASP121 4.6 54.5 1.0
OE2 A:GLU280 4.6 46.9 1.0
OD2 A:ASP121 4.6 53.0 1.0
C A:LEU120 4.7 54.2 1.0
CG A:GLU280 4.8 44.3 1.0
O3 A:FDP401 4.9 48.9 1.0
CZ A:ARG276 5.0 64.8 1.0

Reference:

Y.Gao, L.Shen, R.B.Honzatko. Hydrophobic Central Cavity in Fructose-1,6-Bisphosphatase Is Essential For the Synergism in Amp/Fru 2,6-Bisphosphate Inhibition To Be Published.
Page generated: Fri Aug 16 16:03:35 2024

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