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Magnesium in PDB 6h94: T16A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis with Phosphate and Tris Bound in An Open Conformer to 1.5 A.

Enzymatic activity of T16A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis with Phosphate and Tris Bound in An Open Conformer to 1.5 A.

All present enzymatic activity of T16A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis with Phosphate and Tris Bound in An Open Conformer to 1.5 A.:
5.4.2.6;

Protein crystallography data

The structure of T16A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis with Phosphate and Tris Bound in An Open Conformer to 1.5 A., PDB code: 6h94 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) 33.77 / 1.49
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 50.010, 53.190, 89.940, 90.00, 90.00, 90.00
R / Rfree (%) 19.2 / 21

Magnesium Binding Sites:

The binding sites of Magnesium atom in the T16A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis with Phosphate and Tris Bound in An Open Conformer to 1.5 A. (pdb code 6h94). 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 T16A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis with Phosphate and Tris Bound in An Open Conformer to 1.5 A., PDB code: 6h94:

Magnesium binding site 1 out of 1 in 6h94

Go back to Magnesium Binding Sites List in 6h94
Magnesium binding site 1 out of 1 in the T16A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis with Phosphate and Tris Bound in An Open Conformer to 1.5 A.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of T16A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis with Phosphate and Tris Bound in An Open Conformer to 1.5 A. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg301

b:29.1
occ:1.00
 OD1 A:ASP170 2.1 27.3 1.0
O A:HOH525 2.2 26.7 0.5
O A:ASP10 2.3 24.9 1.0
OD2 A:ASP8 2.3 28.9 1.0
OE1 A:GLU169 2.6 28.2 1.0
CG A:ASP170 3.3 29.6 1.0
CG A:ASP8 3.4 24.9 1.0
O A:HOH466 3.4 33.4 1.0
C A:ASP10 3.4 25.1 1.0
CD A:GLU169 3.7 26.1 1.0
CB A:ASP8 3.8 25.1 1.0
O A:HOH525 3.8 27.6 0.5
O A:HOH411 3.9 40.2 1.0
OE2 A:GLU169 3.9 27.5 1.0
OD2 A:ASP170 3.9 30.5 1.0
N A:ASP170 4.2 25.5 1.0
CB A:ASP10 4.3 24.9 1.0
CA A:ASP10 4.3 24.1 1.0
N A:GLY11 4.4 25.2 1.0
CB A:ASP170 4.4 26.8 1.0
OD1 A:ASP8 4.5 27.2 1.0
O A:HOH502 4.5 36.6 1.0
N A:ASP10 4.5 23.3 1.0
CA A:GLY11 4.5 25.3 1.0
CG2 A:VAL12 4.6 26.4 1.0
OG A:SER171 4.6 30.4 1.0
N A:SER171 4.6 28.9 1.0
CB A:SER171 4.7 29.2 1.0
CA A:ASP170 4.7 27.5 1.0
OD2 A:ASP10 4.8 36.1 1.0
CG A:ASP10 4.9 30.5 1.0
C A:GLY11 4.9 26.0 1.0
C A:ASP170 4.9 28.6 1.0
CG A:GLU169 5.0 23.8 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: Wed Aug 13 06:55:08 2025

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