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Magnesium in PDB 1z4o: Structure of Beta-Phosphoglucomutase with Inhibitor Bound Alpha- Galactose 1-Phosphate

Enzymatic activity of Structure of Beta-Phosphoglucomutase with Inhibitor Bound Alpha- Galactose 1-Phosphate

All present enzymatic activity of Structure of Beta-Phosphoglucomutase with Inhibitor Bound Alpha- Galactose 1-Phosphate:
5.4.2.6;

Protein crystallography data

The structure of Structure of Beta-Phosphoglucomutase with Inhibitor Bound Alpha- Galactose 1-Phosphate, PDB code: 1z4o was solved by L.W.Tremblay, G.Zhang, J.Dai, D.Dunaway-Mariano, K.N.Allen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 55.069, 36.351, 104.883, 90.00, 101.77, 90.00
R / Rfree (%) 19.9 / 25.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Beta-Phosphoglucomutase with Inhibitor Bound Alpha- Galactose 1-Phosphate (pdb code 1z4o). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of Beta-Phosphoglucomutase with Inhibitor Bound Alpha- Galactose 1-Phosphate, PDB code: 1z4o:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1z4o

Go back to Magnesium Binding Sites List in 1z4o
Magnesium binding site 1 out of 2 in the Structure of Beta-Phosphoglucomutase with Inhibitor Bound Alpha- Galactose 1-Phosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Beta-Phosphoglucomutase with Inhibitor Bound Alpha- Galactose 1-Phosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg800

b:20.0
occ:1.00
O A:ASP10 2.1 9.5 1.0
OD2 A:ASP8 2.1 16.6 1.0
O A:HOH1332 2.2 7.6 1.0
OD1 A:ASP170 2.2 15.6 1.0
O A:HOH1250 2.3 22.3 1.0
O A:HOH1476 2.4 27.2 1.0
CG A:ASP8 3.1 15.7 1.0
CG A:ASP170 3.2 17.1 1.0
C A:ASP10 3.3 8.4 1.0
OD2 A:ASP170 3.4 19.5 1.0
OD1 A:ASP8 3.4 14.0 1.0
OE1 A:GLU169 3.9 14.0 1.0
O A:HOH1264 4.0 19.4 1.0
CA A:ASP10 4.1 9.0 1.0
CB A:ASP10 4.2 5.1 1.0
N A:ASP10 4.2 5.7 1.0
N A:GLY11 4.4 9.6 1.0
O6 A:GL11220 4.4 9.4 1.0
CB A:ASP8 4.4 13.0 1.0
CA A:GLY11 4.5 10.0 1.0
CB A:ASP170 4.6 12.1 1.0
O A:HOH1245 4.6 16.0 1.0
OG A:SER171 4.6 17.1 1.0
CA A:GLY46 4.6 10.1 1.0
CD A:GLU169 4.6 12.9 1.0
CB A:SER171 4.7 16.4 1.0
N A:GLY46 4.7 10.0 1.0
N A:ASP170 4.7 11.5 1.0
OE2 A:GLU169 4.7 14.9 1.0
N A:SER171 4.8 14.5 1.0
C A:LEU9 4.9 7.3 1.0
CG2 A:VAL12 4.9 12.2 1.0
C A:GLY11 5.0 10.3 1.0

Magnesium binding site 2 out of 2 in 1z4o

Go back to Magnesium Binding Sites List in 1z4o
Magnesium binding site 2 out of 2 in the Structure of Beta-Phosphoglucomutase with Inhibitor Bound Alpha- Galactose 1-Phosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Beta-Phosphoglucomutase with Inhibitor Bound Alpha- Galactose 1-Phosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg801

b:16.8
occ:1.00
OD2 B:ASP8 2.3 11.7 1.0
O B:ASP10 2.3 18.5 1.0
OD1 B:ASP170 2.3 17.8 1.0
OE1 B:GLU169 2.4 13.2 1.0
O B:HOH1326 2.4 15.5 1.0
CG B:ASP8 3.3 14.0 1.0
CG B:ASP170 3.4 17.0 1.0
O B:HOH1273 3.4 16.2 1.0
CD B:GLU169 3.4 14.2 1.0
C B:ASP10 3.4 17.7 1.0
OE2 B:GLU169 3.8 13.5 1.0
CB B:ASP8 3.8 11.2 1.0
OD2 B:ASP170 4.0 15.0 1.0
O B:HOH1234 4.0 17.6 1.0
N B:ASP170 4.0 13.3 1.0
CA B:ASP10 4.2 17.1 1.0
CB B:ASP10 4.3 20.2 1.0
OG B:SER171 4.4 25.1 1.0
CB B:ASP170 4.4 14.8 1.0
N B:GLY11 4.4 16.0 1.0
OD1 B:ASP8 4.4 13.1 1.0
O B:HOH1292 4.5 26.3 1.0
N B:ASP10 4.5 15.8 1.0
N B:SER171 4.6 20.2 1.0
O B:HOH1296 4.6 26.8 1.0
CA B:GLY11 4.6 16.4 1.0
CA B:ASP170 4.6 16.6 1.0
CG B:GLU169 4.7 13.1 1.0
CB B:SER171 4.8 22.1 1.0
CG2 B:VAL12 4.8 10.5 1.0
O B:HOH1246 4.9 24.9 1.0
C B:ASP170 4.9 18.1 1.0
CA B:GLU169 4.9 11.2 1.0
C B:GLU169 5.0 12.8 1.0

Reference:

L.W.Tremblay, G.Zhang, J.Dai, D.Dunaway-Mariano, K.N.Allen. Chemical Confirmation of A Pentavalent Phosphorane in Complex with Beta-Phosphoglucomutase J.Am.Chem.Soc. V. 127 5298 2005.
ISSN: ISSN 0002-7863
PubMed: 15826149
DOI: 10.1021/JA0509073
Page generated: Tue Aug 13 20:02:22 2024

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