Magnesium in PDB 6hdh: R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 1.6 A.

Enzymatic activity of R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 1.6 A.

All present enzymatic activity of R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 1.6 A.:
5.4.2.6;

Protein crystallography data

The structure of R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 1.6 A., PDB code: 6hdh 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) 31.36 / 1.62
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 38.130, 117.230, 53.010, 90.00, 97.41, 90.00
R / Rfree (%) 18.2 / 21.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 1.6 A. (pdb code 6hdh). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 1.6 A., PDB code: 6hdh:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 6hdh

Go back to Magnesium Binding Sites List in 6hdh
Magnesium binding site 1 out of 2 in the R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 1.6 A.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 1.6 A. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg301

b:26.6
occ:1.00
OD1 A:ASP170 2.2 27.9 1.0
OD2 A:ASP8 2.2 27.5 1.0
O A:HOH487 2.3 31.7 1.0
O A:ASP10 2.3 25.4 1.0
OE1 A:GLU169 2.6 27.5 1.0
CG A:ASP8 3.3 25.5 1.0
CG A:ASP170 3.4 29.1 1.0
O A:HOH438 3.4 32.6 1.0
C A:ASP10 3.5 22.9 1.0
CD A:GLU169 3.5 28.0 1.0
CB A:ASP8 3.8 24.9 1.0
O A:HOH412 3.9 27.9 1.0
OE2 A:GLU169 3.9 25.2 1.0
OD2 A:ASP170 4.0 28.2 1.0
N A:ASP170 4.1 22.5 1.0
O A:HOH426 4.4 34.7 1.0
OD1 A:ASP8 4.4 23.9 1.0
N A:GLY11 4.4 22.8 1.0
CB A:ASP170 4.4 25.8 1.0
CA A:GLY11 4.4 24.0 1.0
CA A:ASP10 4.5 22.2 1.0
CB A:ASP10 4.6 26.0 1.0
OG A:SER171 4.6 28.3 1.0
CG2 A:VAL12 4.6 23.1 1.0
N A:ASP10 4.6 21.8 1.0
N A:SER171 4.7 25.5 1.0
CB A:SER171 4.7 28.3 1.0
CA A:ASP170 4.7 24.3 1.0
CG A:GLU169 4.8 25.6 1.0
C A:GLY11 4.8 23.4 1.0
CA A:GLU169 4.9 22.5 1.0
C A:ASP170 5.0 27.3 1.0

Magnesium binding site 2 out of 2 in 6hdh

Go back to Magnesium Binding Sites List in 6hdh
Magnesium binding site 2 out of 2 in the R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 1.6 A.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 1.6 A. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg301

b:28.8
occ:1.00
OD1 B:ASP170 2.2 28.9 1.0
OD2 B:ASP8 2.2 26.7 1.0
O B:HOH484 2.2 37.5 1.0
O B:ASP10 2.4 26.1 1.0
OE1 B:GLU169 2.6 27.5 1.0
CG B:ASP8 3.3 24.3 1.0
O B:HOH430 3.3 31.9 1.0
CG B:ASP170 3.4 30.2 1.0
CD B:GLU169 3.5 24.1 1.0
C B:ASP10 3.6 24.5 1.0
CB B:ASP8 3.8 22.1 1.0
OE2 B:GLU169 3.9 26.1 1.0
N B:ASP170 4.0 23.1 1.0
OD2 B:ASP170 4.1 30.0 1.0
OD1 B:ASP8 4.4 24.9 1.0
O B:HOH473 4.4 42.1 1.0
CB B:ASP170 4.4 25.5 1.0
N B:GLY11 4.5 22.6 1.0
CA B:ASP10 4.5 24.1 1.0
CA B:GLY11 4.5 22.6 1.0
OG B:SER171 4.6 25.3 1.0
CG2 B:VAL12 4.6 23.4 1.0
N B:SER171 4.6 22.8 1.0
N B:ASP10 4.6 23.3 1.0
CB B:SER171 4.6 24.9 1.0
CB B:ASP10 4.6 26.4 1.0
CA B:ASP170 4.7 22.4 1.0
CG B:GLU169 4.8 21.8 1.0
C B:ASP170 4.9 25.4 1.0
CA B:GLU169 4.9 20.2 1.0
C B:GLY11 4.9 23.4 1.0
C B:GLU169 5.0 22.9 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: Mon Dec 14 22:48:56 2020

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