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Magnesium in PDB 7c9q: Crystal Structure of Human Liver Fructose-1,6-Bisphoaphatase Complex with MG2+ and Amp

Enzymatic activity of Crystal Structure of Human Liver Fructose-1,6-Bisphoaphatase Complex with MG2+ and Amp

All present enzymatic activity of Crystal Structure of Human Liver Fructose-1,6-Bisphoaphatase Complex with MG2+ and Amp:
3.1.3.11;

Protein crystallography data

The structure of Crystal Structure of Human Liver Fructose-1,6-Bisphoaphatase Complex with MG2+ and Amp, PDB code: 7c9q was solved by Y.Huang, R.Li, J.Wan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.69 / 1.88
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 67.361, 83.286, 276.544, 90, 90, 90
R / Rfree (%) 18.2 / 21.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Human Liver Fructose-1,6-Bisphoaphatase Complex with MG2+ and Amp (pdb code 7c9q). 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 Human Liver Fructose-1,6-Bisphoaphatase Complex with MG2+ and Amp, PDB code: 7c9q:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 7c9q

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Magnesium binding site 1 out of 4 in the Crystal Structure of Human Liver Fructose-1,6-Bisphoaphatase Complex with MG2+ and Amp


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 Human Liver Fructose-1,6-Bisphoaphatase Complex with MG2+ and Amp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:14.3
occ:1.00
 OE2 A:GLU98 2.2 26.3 1.0
OE1 A:GLU97 2.3 24.5 1.0
O A:LEU120 2.3 25.9 1.0
O A:HOH537 2.3 25.0 1.0
OD1 A:ASP118 2.4 17.8 1.0
O A:HOH632 2.4 25.8 1.0
CD A:GLU97 3.2 26.6 1.0
CD A:GLU98 3.3 28.6 1.0
CG A:ASP118 3.3 19.9 1.0
C A:LEU120 3.5 24.0 1.0
OD2 A:ASP118 3.6 23.5 1.0
OE2 A:GLU97 4.0 27.1 1.0
OE1 A:GLU98 4.0 29.1 1.0
CA A:ASP121 4.0 21.8 1.0
CG A:GLU97 4.0 20.1 1.0
CB A:GLU97 4.2 22.8 1.0
N A:ASP121 4.2 23.4 1.0
CG A:GLU98 4.3 23.5 1.0
N A:LEU120 4.4 18.1 1.0
OD1 A:ASP74 4.6 28.7 1.0
CA A:LEU120 4.6 21.3 1.0
CD A:PRO119 4.7 16.5 1.0
CB A:ASP118 4.7 17.6 1.0
O A:HOH545 4.7 31.6 1.0
CG A:ASP74 4.8 29.2 1.0
CB A:ASP121 4.8 23.8 1.0
OG A:SER124 4.9 45.1 1.0
C A:ASP121 5.0 26.4 1.0
N A:PRO119 5.0 16.7 1.0

Magnesium binding site 2 out of 4 in 7c9q

Go back to Magnesium Binding Sites List in 7c9q
Magnesium binding site 2 out of 4 in the Crystal Structure of Human Liver Fructose-1,6-Bisphoaphatase Complex with MG2+ and Amp


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 Human Liver Fructose-1,6-Bisphoaphatase Complex with MG2+ and Amp within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg402

b:33.1
occ:1.00
 OE2 C:GLU280 2.1 38.5 1.0
OD1 C:ASP121 2.2 35.5 1.0
OD2 C:ASP118 2.3 36.6 1.0
OE2 C:GLU97 2.6 39.8 1.0
O C:HOH632 3.1 47.7 1.0
CG C:ASP121 3.3 34.8 1.0
CD C:GLU97 3.3 40.1 1.0
CD C:GLU280 3.3 31.5 1.0
CG C:ASP118 3.3 28.6 1.0
OE1 C:GLU97 3.4 51.8 1.0
OD1 C:ASP118 3.9 30.0 1.0
CB C:ASP121 3.9 31.9 1.0
CA C:ASP121 4.0 32.7 1.0
OE1 C:GLU280 4.2 30.0 1.0
CG C:GLU280 4.2 25.8 1.0
OD2 C:ASP121 4.3 37.7 1.0
CB C:ASP118 4.4 25.0 1.0
O C:HOH521 4.5 39.7 1.0
CG C:GLU97 4.7 35.6 1.0
N C:GLY122 4.8 34.9 1.0
N C:ASP121 4.9 30.7 1.0
C C:ASP121 5.0 33.6 1.0

Magnesium binding site 3 out of 4 in 7c9q

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Magnesium binding site 3 out of 4 in the Crystal Structure of Human Liver Fructose-1,6-Bisphoaphatase Complex with MG2+ and Amp


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 Human Liver Fructose-1,6-Bisphoaphatase Complex with MG2+ and Amp within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg402

b:43.6
occ:1.00
 OD1 D:ASP121 2.0 40.5 1.0
OE2 D:GLU280 2.3 39.0 1.0
OD2 D:ASP118 2.4 41.9 1.0
OE1 D:GLU97 2.6 48.0 1.0
O D:HOH612 2.9 49.3 1.0
O D:HOH583 3.0 48.4 1.0
OE2 D:GLU97 3.2 55.1 1.0
CG D:ASP121 3.2 39.7 1.0
CD D:GLU97 3.2 49.5 1.0
CG D:ASP118 3.4 34.3 1.0
CD D:GLU280 3.5 36.2 1.0
CB D:ASP121 3.8 34.8 1.0
OD1 D:ASP118 3.8 33.9 1.0
CA D:ASP121 3.9 33.8 1.0
O D:HOH540 4.0 42.2 1.0
OD2 D:ASP121 4.2 43.6 1.0
CG D:GLU280 4.3 35.3 1.0
OE1 D:GLU280 4.4 33.5 1.0
N D:GLY122 4.7 40.4 1.0
CB D:ASP118 4.7 27.9 1.0
CG D:GLU97 4.7 40.9 1.0
C D:ASP121 4.9 34.5 1.0
N D:ASP121 4.9 29.7 1.0
O D:HOH511 5.0 42.4 1.0

Magnesium binding site 4 out of 4 in 7c9q

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Magnesium binding site 4 out of 4 in the Crystal Structure of Human Liver Fructose-1,6-Bisphoaphatase Complex with MG2+ and Amp


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 Human Liver Fructose-1,6-Bisphoaphatase Complex with MG2+ and Amp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg402

b:22.0
occ:1.00
 O B:LEU120 2.1 32.8 1.0
OE2 B:GLU98 2.2 35.6 1.0
O B:HOH614 2.3 32.4 1.0
O B:HOH521 2.3 29.1 1.0
OD1 B:ASP118 2.4 26.8 1.0
OE1 B:GLU97 2.5 33.1 1.0
C B:LEU120 3.3 25.8 1.0
CD B:GLU97 3.3 35.2 1.0
CG B:ASP118 3.4 24.8 1.0
CD B:GLU98 3.4 33.3 1.0
OD2 B:ASP118 3.7 25.6 1.0
CA B:ASP121 4.0 34.6 1.0
OE2 B:GLU97 4.1 38.3 1.0
N B:ASP121 4.1 30.1 1.0
CB B:GLU97 4.1 22.6 1.0
CG B:GLU97 4.1 28.4 1.0
O B:HOH699 4.1 42.8 1.0
OE1 B:GLU98 4.2 32.1 1.0
N B:LEU120 4.2 18.8 1.0
O B:HOH618 4.2 47.0 1.0
CG B:GLU98 4.3 29.1 1.0
CA B:LEU120 4.4 22.3 1.0
OD2 B:ASP74 4.5 39.3 1.0
O B:HOH507 4.5 42.7 1.0
CD B:PRO119 4.5 19.2 1.0
O B:HOH502 4.6 38.4 1.0
CB B:ASP118 4.7 18.9 1.0
CG B:ASP74 4.7 36.0 1.0
CB B:ASP121 4.9 27.2 1.0
N B:PRO119 4.9 18.4 1.0
CG B:PRO119 5.0 20.4 1.0

Reference:

Y.Huang, R.Li, J.Wan. Crystal Structure of Human Liver Fructose-1,6-Bisphoaphatase Complex with MG2+ and Amp To Be Published.
Page generated: Wed Oct 2 13:53:48 2024

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