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Magnesium in PDB 6hdm: R49A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed with Magnesium Trifluoride and Beta-G6P to 1.3 A.

Enzymatic activity of R49A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed with Magnesium Trifluoride and Beta-G6P to 1.3 A.

All present enzymatic activity of R49A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed with Magnesium Trifluoride and Beta-G6P to 1.3 A.:
5.4.2.6;

Protein crystallography data

The structure of R49A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed with Magnesium Trifluoride and Beta-G6P to 1.3 A., PDB code: 6hdm 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) 48.27 / 1.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 37.300, 54.340, 104.620, 90.00, 90.00, 90.00
R / Rfree (%) 12.6 / 14.8

Other elements in 6hdm:

The structure of R49A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed with Magnesium Trifluoride and Beta-G6P 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 R49A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed with Magnesium Trifluoride and Beta-G6P to 1.3 A. (pdb code 6hdm). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the R49A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed with Magnesium Trifluoride and Beta-G6P to 1.3 A., PDB code: 6hdm:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 6hdm

Go back to Magnesium Binding Sites List in 6hdm
Magnesium binding site 1 out of 2 in the R49A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed with Magnesium Trifluoride and Beta-G6P 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 R49A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed with Magnesium Trifluoride and Beta-G6P to 1.3 A. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg301

b:8.4
occ:1.00
 F3 A:MGF302 1.9 8.6 1.0
OD2 A:ASP8 2.0 8.6 1.0
OD1 A:ASP170 2.1 8.7 1.0
O A:ASP10 2.1 8.1 1.0
O A:HOH495 2.1 10.4 1.0
O A:HOH435 2.1 8.6 1.0
CG A:ASP8 3.0 8.2 1.0
CG A:ASP170 3.0 8.5 1.0
C A:ASP10 3.3 6.8 1.0
OD2 A:ASP170 3.4 9.2 1.0
OD1 A:ASP8 3.4 8.4 1.0
MG A:MGF302 3.5 8.1 1.0
O2 A:BG6304 3.8 9.0 1.0
CA A:ASP10 4.0 7.0 1.0
OE1 A:GLU169 4.1 13.3 1.0
N A:ASP10 4.1 7.2 1.0
CB A:ASP10 4.1 7.2 1.0
N A:GLY11 4.3 7.1 1.0
CB A:ASP8 4.3 8.2 1.0
CB A:ASP170 4.4 8.7 1.0
F2 A:MGF302 4.5 8.3 1.0
O A:HOH512 4.6 10.4 1.0
CA A:GLY11 4.6 7.7 1.0
N A:ASP170 4.6 8.5 1.0
CD A:GLU169 4.7 10.6 1.0
CB A:SER171 4.7 11.0 1.0
OE2 A:GLU169 4.7 14.8 1.0
F1 A:MGF302 4.7 15.2 1.0
O1 A:BG6304 4.7 8.1 1.0
OG A:SER171 4.8 11.7 1.0
N A:GLY46 4.8 10.1 1.0
C A:LEU9 4.8 7.0 1.0
CG2 A:VAL12 4.9 9.3 1.0
CA A:ASP170 4.9 8.8 1.0
CA A:GLY46 5.0 10.7 1.0

Magnesium binding site 2 out of 2 in 6hdm

Go back to Magnesium Binding Sites List in 6hdm
Magnesium binding site 2 out of 2 in the R49A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed with Magnesium Trifluoride and Beta-G6P to 1.3 A.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of R49A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed with Magnesium Trifluoride and Beta-G6P to 1.3 A. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg302

b:8.1
occ:1.00
 MG A:MGF302 0.0 8.1 1.0
F1 A:MGF302 1.9 15.2 1.0
F2 A:MGF302 1.9 8.3 1.0
F3 A:MGF302 1.9 8.6 1.0
OD1 A:ASP8 2.0 8.4 1.0
O1 A:BG6304 2.1 8.1 1.0
CG A:ASP8 3.0 8.2 1.0
C1 A:BG6304 3.2 8.2 1.0
OD2 A:ASP8 3.4 8.6 1.0
MG A:MG301 3.5 8.4 1.0
O A:HOH495 3.6 10.4 1.0
O2 A:BG6304 3.6 9.0 1.0
OG A:SER114 3.7 10.2 1.0
NZ A:LYS145 3.8 10.6 1.0
N A:ASP10 3.9 7.2 1.0
OD2 A:ASP10 3.9 8.6 1.0
C2 A:BG6304 3.9 8.5 1.0
N A:ALA115 4.0 13.3 1.0
N A:LEU9 4.0 7.5 1.0
CA A:SER114 4.0 12.6 1.0
CB A:ASP10 4.2 7.2 1.0
CB A:SER114 4.2 10.6 1.0
O5 A:BG6304 4.3 8.2 1.0
CB A:ASP8 4.3 8.2 1.0
CG A:ASP10 4.4 8.0 1.0
O A:ASP10 4.4 8.1 1.0
CA A:ASP10 4.5 7.0 1.0
C A:SER114 4.6 11.3 1.0
CA A:ASP8 4.7 8.1 1.0
C A:LEU9 4.7 7.0 1.0
O A:HOH435 4.8 8.6 1.0
CA A:GLY46 4.8 10.7 1.0
CA A:LEU9 4.8 7.1 1.0
OE2 A:GLU169 4.8 14.8 1.0
C A:ASP8 4.9 7.7 1.0
CB A:ALA115 4.9 17.2 1.0
CE A:LYS145 5.0 11.0 1.0
CA A:ALA115 5.0 13.4 1.0
N A:SER116 5.0 9.4 1.0
C A:ASP10 5.0 6.8 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: Tue Oct 1 01:41:59 2024

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