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Magnesium in PDB 2fhy: Structure of Human Liver Fpbase Complexed with A Novel Benzoxazole As Allosteric Inhibitor

Enzymatic activity of Structure of Human Liver Fpbase Complexed with A Novel Benzoxazole As Allosteric Inhibitor

All present enzymatic activity of Structure of Human Liver Fpbase Complexed with A Novel Benzoxazole As Allosteric Inhibitor:
3.1.3.11;

Protein crystallography data

The structure of Structure of Human Liver Fpbase Complexed with A Novel Benzoxazole As Allosteric Inhibitor, PDB code: 2fhy was solved by C.Abad-Zapatero, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.89 / 2.95
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 83.748, 109.126, 190.838, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Other elements in 2fhy:

The structure of Structure of Human Liver Fpbase Complexed with A Novel Benzoxazole As Allosteric Inhibitor also contains other interesting chemical elements:

Chlorine (Cl) 12 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Human Liver Fpbase Complexed with A Novel Benzoxazole As Allosteric Inhibitor (pdb code 2fhy). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Structure of Human Liver Fpbase Complexed with A Novel Benzoxazole As Allosteric Inhibitor, PDB code: 2fhy:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 2fhy

Go back to Magnesium Binding Sites List in 2fhy
Magnesium binding site 1 out of 4 in the Structure of Human Liver Fpbase Complexed with A Novel Benzoxazole As Allosteric Inhibitor


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Human Liver Fpbase Complexed with A Novel Benzoxazole As Allosteric Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:21.1
occ:1.00
 OE1 A:GLU97 2.5 79.9 1.0
OE1 A:GLU280 2.5 91.9 1.0
OD2 A:ASP118 2.5 58.1 1.0
OE2 A:GLU97 2.7 81.9 1.0
OD1 A:ASP121 2.7 73.8 1.0
CD A:GLU97 2.9 83.3 1.0
CG A:ASP118 3.4 62.9 1.0
OD1 A:ASP118 3.5 65.3 1.0
CG A:ASP121 3.7 79.3 1.0
CD A:GLU280 3.8 88.6 1.0
CA A:ASP121 4.0 58.8 1.0
CB A:ASP121 4.0 75.9 1.0
O A:LEU120 4.4 76.5 1.0
CG A:GLU97 4.4 77.3 1.0
OE2 A:GLU280 4.6 81.9 1.0
N A:GLY122 4.7 86.5 1.0
CG A:GLU280 4.7 80.5 1.0
OD2 A:ASP121 4.7 72.8 1.0
CB A:ASP118 4.8 57.9 1.0
C A:ASP121 4.9 64.5 1.0
N A:ASP121 5.0 61.0 1.0

Magnesium binding site 2 out of 4 in 2fhy

Go back to Magnesium Binding Sites List in 2fhy
Magnesium binding site 2 out of 4 in the Structure of Human Liver Fpbase Complexed with A Novel Benzoxazole As Allosteric Inhibitor


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Human Liver Fpbase Complexed with A Novel Benzoxazole As Allosteric Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg601

b:21.1
occ:1.00
 OD2 D:ASP118 2.4 83.3 1.0
OE1 D:GLU280 2.4 79.3 1.0
OE1 D:GLU97 2.4 82.0 1.0
OD1 D:ASP121 2.7 66.4 1.0
OE2 D:GLU97 2.7 85.8 1.0
CD D:GLU97 2.9 86.0 1.0
CG D:ASP118 3.3 77.3 1.0
OD1 D:ASP118 3.4 83.4 1.0
CG D:ASP121 3.6 73.5 1.0
CD D:GLU280 3.7 73.3 1.0
CB D:ASP121 4.0 66.5 1.0
CA D:ASP121 4.0 68.3 1.0
O D:LEU120 4.4 81.3 1.0
CG D:GLU97 4.4 78.1 1.0
OE2 D:GLU280 4.5 69.8 1.0
CG D:GLU280 4.5 68.5 1.0
CB D:ASP118 4.7 71.1 1.0
OD2 D:ASP121 4.7 70.2 1.0
N D:GLY122 4.7 38.0 1.0
CB D:GLU97 4.9 77.3 1.0
N D:ASP121 5.0 61.2 1.0
C D:ASP121 5.0 73.2 1.0

Magnesium binding site 3 out of 4 in 2fhy

Go back to Magnesium Binding Sites List in 2fhy
Magnesium binding site 3 out of 4 in the Structure of Human Liver Fpbase Complexed with A Novel Benzoxazole As Allosteric Inhibitor


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structure of Human Liver Fpbase Complexed with A Novel Benzoxazole As Allosteric Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Mg701

b:21.1
occ:1.00
 OD2 H:ASP118 2.4 63.6 1.0
OE1 H:GLU280 2.4 0.1 1.0
OD1 H:ASP121 2.5 84.7 1.0
OE1 H:GLU97 2.6 98.6 1.0
OE2 H:GLU97 2.8 0.1 1.0
CD H:GLU97 3.0 0.9 1.0
CG H:ASP118 3.3 58.5 1.0
OD1 H:ASP118 3.5 61.6 1.0
CG H:ASP121 3.5 90.3 1.0
CD H:GLU280 3.7 0.7 1.0
CB H:ASP121 3.9 91.5 1.0
CA H:ASP121 3.9 72.4 1.0
O H:LEU120 4.3 60.1 1.0
OE2 H:GLU280 4.5 96.6 1.0
CG H:GLU97 4.5 95.3 1.0
OD2 H:ASP121 4.6 91.0 1.0
CG H:GLU280 4.6 89.0 1.0
N H:GLY122 4.6 88.4 1.0
CB H:ASP118 4.7 56.5 1.0
C H:ASP121 4.8 81.2 1.0
N H:ASP121 4.9 63.6 1.0

Magnesium binding site 4 out of 4 in 2fhy

Go back to Magnesium Binding Sites List in 2fhy
Magnesium binding site 4 out of 4 in the Structure of Human Liver Fpbase Complexed with A Novel Benzoxazole As Allosteric Inhibitor


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Structure of Human Liver Fpbase Complexed with A Novel Benzoxazole As Allosteric Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
L:Mg801

b:21.1
occ:1.00
 OE1 L:GLU280 2.4 72.3 1.0
OD2 L:ASP118 2.4 74.5 1.0
OE1 L:GLU97 2.5 80.3 1.0
OD1 L:ASP121 2.6 95.4 1.0
OE2 L:GLU97 2.7 81.4 1.0
CD L:GLU97 2.9 81.2 1.0
CG L:ASP118 3.4 67.2 1.0
OD1 L:ASP118 3.5 69.3 1.0
CG L:ASP121 3.6 91.9 1.0
CD L:GLU280 3.7 64.8 1.0
CB L:ASP121 4.0 83.2 1.0
CA L:ASP121 4.0 78.1 1.0
CG L:GLU97 4.4 72.9 1.0
O L:LEU120 4.4 78.2 1.0
OE2 L:GLU280 4.5 59.3 1.0
CG L:GLU280 4.6 64.6 1.0
OD2 L:ASP121 4.7 90.5 1.0
N L:GLY122 4.7 0.5 1.0
CB L:ASP118 4.8 61.1 1.0
C L:ASP121 5.0 81.6 1.0
CB L:GLU97 5.0 61.5 1.0
N L:ASP121 5.0 63.3 1.0

Reference:

T.W.Von Geldern, C.Lai, R.J.Gum, M.Daly, C.Sun, E.H.Fry, C.Abad-Zapatero. Benzoxazole Benzenesulfonamides Are Novel Allosteric Inhibitors of Fructose-1,6-Bisphosphatase with A Distinct Binding Mode. Bioorg.Med.Chem.Lett. V. 16 1811 2006.
ISSN: ISSN 0960-894X
PubMed: 16442285
DOI: 10.1016/J.BMCL.2006.01.015
Page generated: Mon Dec 14 07:22:53 2020

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