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Magnesium in PDB 6h90: K145A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited By Beryllium Trifluoride to 1.3 A.

Enzymatic activity of K145A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited By Beryllium Trifluoride to 1.3 A.

All present enzymatic activity of K145A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited By Beryllium Trifluoride to 1.3 A.:
5.4.2.6;

Protein crystallography data

The structure of K145A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited By Beryllium Trifluoride to 1.3 A., PDB code: 6h90 was solved by A.J.Robertson, C.Bisson, J.P.Waltho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.75 / 1.31
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 52.320, 53.630, 81.500, 90.00, 90.00, 90.00
R / Rfree (%) 13.5 / 16.3

Other elements in 6h90:

The structure of K145A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited By Beryllium Trifluoride to 1.3 A. also contains other interesting chemical elements:

Fluorine (F) 3 atoms
Sodium (Na) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the K145A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited By Beryllium Trifluoride to 1.3 A. (pdb code 6h90). 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 K145A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited By Beryllium Trifluoride to 1.3 A., PDB code: 6h90:

Magnesium binding site 1 out of 1 in 6h90

Go back to Magnesium Binding Sites List in 6h90
Magnesium binding site 1 out of 1 in the K145A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited By Beryllium Trifluoride to 1.3 A.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of K145A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited By Beryllium Trifluoride to 1.3 A. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg301

b:10.8
occ:1.00
 F2 A:BEF303 2.0 10.3 1.0
OD2 A:ASP8 2.0 10.2 1.0
O A:ASP10 2.1 10.8 1.0
O A:HOH433 2.1 12.6 1.0
OD1 A:ASP170 2.1 11.2 1.0
O A:HOH481 2.1 11.5 1.0
CG A:ASP8 3.0 9.9 1.0
CG A:ASP170 3.1 11.6 1.0
BE A:BEF303 3.2 10.6 1.0
C A:ASP10 3.2 10.1 1.0
OD2 A:ASP170 3.4 12.6 1.0
OD1 A:ASP8 3.4 10.0 1.0
OE1 A:GLU169 3.9 12.4 1.0
CA A:ASP10 4.0 10.5 1.0
CB A:ASP10 4.0 12.3 1.0
N A:ASP10 4.1 9.5 1.0
OD2 A:ASP10 4.2 22.8 1.0
O A:HOH632 4.2 20.5 1.0
F3 A:BEF303 4.2 11.0 1.0
N A:GLY11 4.3 10.8 1.0
F1 A:BEF303 4.3 12.8 1.0
CB A:ASP8 4.4 9.9 1.0
CB A:ASP170 4.4 11.3 1.0
CG A:ASP10 4.5 17.5 1.0
CD A:GLU169 4.5 11.5 1.0
CA A:GLY11 4.5 11.4 1.0
N A:ASP170 4.5 10.7 1.0
OE2 A:GLU169 4.5 12.7 1.0
C A:LEU9 4.9 8.9 1.0
CA A:ASP170 4.9 10.9 1.0

Reference:

A.J.Robertson, C.Bisson, J.P.Waltho. Transition State of Phospho-Enzyme Hydrolysis in Beta-Phosphoglucomutase. To Be Published.
Page generated: Tue Oct 1 01:36:37 2024

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