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Magnesium in PDB 6h8x: Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Magnesium Trifluoride to 1.8 A.

Enzymatic activity of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Magnesium Trifluoride to 1.8 A.

All present enzymatic activity of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Magnesium Trifluoride to 1.8 A.:
5.4.2.6;

Protein crystallography data

The structure of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Magnesium Trifluoride to 1.8 A., PDB code: 6h8x 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) 23.31 / 1.83
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 38.160, 116.980, 53.110, 90.00, 98.93, 90.00
R / Rfree (%) 18.3 / 22.6

Other elements in 6h8x:

The structure of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Magnesium Trifluoride to 1.8 A. also contains other interesting chemical elements:

Fluorine (F) 6 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Magnesium Trifluoride to 1.8 A. (pdb code 6h8x). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Magnesium Trifluoride to 1.8 A., PDB code: 6h8x:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 6h8x

Go back to Magnesium Binding Sites List in 6h8x
Magnesium binding site 1 out of 4 in the Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Magnesium Trifluoride to 1.8 A.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Magnesium Trifluoride to 1.8 A. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg301

b:29.0
occ:1.00
 OD2 A:ASP8 1.9 30.4 1.0
O A:HOH460 2.0 28.2 1.0
OD1 A:ASP170 2.0 22.8 1.0
O A:ASP10 2.1 21.2 1.0
F1 A:MGF305 2.1 38.0 1.0
O A:HOH403 2.3 28.0 1.0
CG A:ASP8 3.0 26.4 1.0
CG A:ASP170 3.1 26.8 1.0
C A:ASP10 3.3 21.5 1.0
OD2 A:ASP170 3.5 26.4 1.0
OD1 A:ASP8 3.6 27.7 1.0
OE1 A:GLU169 3.6 25.8 1.0
MG A:MGF305 3.9 38.8 1.0
CA A:ASP10 4.2 20.6 1.0
N A:GLY11 4.2 22.6 1.0
CB A:ASP10 4.2 22.3 1.0
CB A:ASP8 4.2 24.3 1.0
CD A:GLU169 4.3 25.5 1.0
OD2 A:ASP10 4.3 29.7 1.0
N A:ASP10 4.4 20.0 1.0
CA A:GLY11 4.4 21.9 1.0
CB A:ASP170 4.4 25.3 1.0
OE2 A:GLU169 4.4 24.3 1.0
N A:ASP170 4.4 25.0 1.0
CG A:ASP10 4.7 24.7 1.0
N A:SER171 4.7 28.9 1.0
CB A:SER171 4.7 28.9 1.0
C A:GLY11 4.9 25.1 1.0
CG2 A:VAL12 4.9 26.1 1.0
CA A:ASP170 4.9 25.6 1.0
OG A:SER171 4.9 29.3 1.0
F3 A:MGF305 4.9 32.8 1.0
C A:LEU9 5.0 20.9 1.0

Magnesium binding site 2 out of 4 in 6h8x

Go back to Magnesium Binding Sites List in 6h8x
Magnesium binding site 2 out of 4 in the Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Magnesium Trifluoride to 1.8 A.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Magnesium Trifluoride to 1.8 A. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg305

b:38.8
occ:1.00
 MG A:MGF305 0.0 38.8 1.0
F1 A:MGF305 2.0 38.0 1.0
F3 A:MGF305 2.0 32.8 1.0
F2 A:MGF305 2.0 33.8 1.0
OD1 A:ASP8 2.4 27.7 1.0
CG A:ASP8 3.4 26.4 1.0
CH3 A:ACT306 3.7 48.5 1.0
OD2 A:ASP8 3.7 30.4 1.0
O A:HOH460 3.9 28.2 1.0
OG A:SER114 3.9 18.3 1.0
MG A:MG301 3.9 29.0 1.0
NZ A:LYS145 4.0 23.3 1.0
N A:ASP10 4.1 20.0 1.0
CB A:ASP10 4.2 22.3 1.0
N A:ALA115 4.3 20.5 1.0
N A:LEU9 4.4 20.4 1.0
OXT A:ACT306 4.6 48.4 1.0
O A:ASP10 4.6 21.2 1.0
CB A:SER114 4.6 18.7 1.0
CA A:SER114 4.6 19.1 1.0
C A:ACT306 4.7 51.5 1.0
CA A:ASP10 4.7 20.6 1.0
CB A:ASP8 4.8 24.3 1.0
O A:HOH403 4.8 28.0 1.0
CB A:ALA115 4.9 24.9 1.0
OE2 A:GLU169 5.0 24.3 1.0
C A:LEU9 5.0 20.9 1.0

Magnesium binding site 3 out of 4 in 6h8x

Go back to Magnesium Binding Sites List in 6h8x
Magnesium binding site 3 out of 4 in the Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Magnesium Trifluoride to 1.8 A.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Magnesium Trifluoride to 1.8 A. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg301

b:27.2
occ:1.00
 F2 B:MGF308 1.9 33.5 1.0
OD2 B:ASP8 2.0 30.8 1.0
OD1 B:ASP170 2.0 24.8 1.0
O B:HOH408 2.1 30.4 1.0
O B:HOH432 2.1 29.1 1.0
O B:ASP10 2.2 24.6 1.0
CG B:ASP170 3.1 25.7 1.0
CG B:ASP8 3.1 24.2 1.0
C B:ASP10 3.3 22.5 1.0
OD2 B:ASP170 3.5 26.8 1.0
OE1 B:GLU169 3.5 27.3 1.0
OD1 B:ASP8 3.6 24.7 1.0
MG B:MGF308 3.7 37.5 1.0
CA B:ASP10 4.1 22.1 1.0
CB B:ASP10 4.2 24.1 1.0
N B:GLY11 4.3 22.8 1.0
OD2 B:ASP10 4.3 27.8 1.0
CB B:ASP8 4.4 21.6 1.0
CD B:GLU169 4.4 25.5 1.0
CB B:ASP170 4.4 22.9 1.0
N B:ASP10 4.4 20.5 1.0
N B:ASP170 4.4 23.5 1.0
CA B:GLY11 4.5 23.8 1.0
OE2 B:GLU169 4.5 25.4 1.0
O B:HOH495 4.6 36.1 1.0
CG B:ASP10 4.7 26.4 1.0
CB B:SER171 4.7 25.2 1.0
OG B:SER171 4.7 26.5 1.0
CA B:ASP170 4.8 23.1 1.0
N B:SER171 4.9 25.7 1.0
CG2 B:VAL12 4.9 23.3 1.0
F1 B:MGF308 4.9 33.7 1.0
C B:GLY11 5.0 23.3 1.0
C B:ASP170 5.0 25.3 1.0

Magnesium binding site 4 out of 4 in 6h8x

Go back to Magnesium Binding Sites List in 6h8x
Magnesium binding site 4 out of 4 in the Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Magnesium Trifluoride to 1.8 A.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Magnesium Trifluoride to 1.8 A. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg308

b:37.5
occ:1.00
 MG B:MGF308 0.0 37.5 1.0
O B:HOH495 1.7 36.1 1.0
F1 B:MGF308 2.0 33.7 1.0
F2 B:MGF308 2.0 33.5 1.0
F3 B:MGF308 2.0 34.1 1.0
OD1 B:ASP8 2.1 24.7 1.0
CG B:ASP8 3.0 24.2 1.0
OD2 B:ASP8 3.3 30.8 1.0
MG B:MG301 3.7 27.2 1.0
OG B:SER114 3.8 19.3 1.0
NZ B:LYS145 3.9 24.3 1.0
O B:HOH408 3.9 30.4 1.0
N B:ASP10 3.9 20.5 1.0
O B:HOH493 3.9 49.0 1.0
N B:LEU9 4.2 19.9 1.0
CB B:ASP10 4.2 24.1 1.0
N B:ALA115 4.3 21.2 1.0
O B:ASP10 4.4 24.6 1.0
CB B:ASP8 4.4 21.6 1.0
CA B:ASP10 4.5 22.1 1.0
CB B:SER114 4.6 20.1 1.0
CA B:SER114 4.6 21.0 1.0
O B:HOH432 4.7 29.1 1.0
C B:LEU9 4.8 20.5 1.0
OE2 B:GLU169 4.9 25.4 1.0
CA B:LEU9 4.9 21.8 1.0
CA B:ASP8 4.9 20.0 1.0
C B:ASP10 4.9 22.5 1.0
CE B:LYS145 5.0 25.6 1.0
CB B:LEU9 5.0 24.4 1.0
CB B:ALA115 5.0 23.0 1.0
C B:ASP8 5.0 20.8 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 01:35:47 2024

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