Atomistry » Magnesium » PDB 2f6w-2fl0 » 2fhy
Atomistry »
  Magnesium »
    PDB 2f6w-2fl0 »
      2fhy »

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

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy