Magnesium in PDB 6h91: Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.4 A

Enzymatic activity of Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.4 A

All present enzymatic activity of Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.4 A:
5.4.2.6;

Protein crystallography data

The structure of Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.4 A, PDB code: 6h91 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) 58.62 / 2.38
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 38.330, 117.230, 52.930, 90.00, 97.75, 90.00
R / Rfree (%) 21.9 / 29.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.4 A (pdb code 6h91). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.4 A, PDB code: 6h91:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 6h91

Go back to Magnesium Binding Sites List in 6h91
Magnesium binding site 1 out of 2 in the Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.4 A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.4 A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg301

b:26.9
occ:1.00
O A:HOH410 1.9 16.8 1.0
O A:HOH412 2.0 30.3 1.0
OP1 A:PHD8 2.0 26.1 1.0
OD1 A:ASP170 2.1 31.2 1.0
O A:ASP10 2.2 32.8 1.0
OD2 A:PHD8 2.2 27.4 1.0
CG A:ASP170 3.1 33.2 1.0
CG A:PHD8 3.1 28.1 1.0
C A:ASP10 3.3 32.0 1.0
P A:PHD8 3.3 26.6 1.0
OD2 A:ASP170 3.3 29.9 1.0
OD1 A:PHD8 3.5 27.7 1.0
OE1 A:GLU169 3.9 37.6 1.0
O A:HOH411 4.0 29.8 1.0
CB A:ASP10 4.0 29.9 1.0
CA A:ASP10 4.0 30.3 1.0
OD2 A:ASP10 4.1 32.5 1.0
OP2 A:PHD8 4.2 26.7 1.0
OP3 A:PHD8 4.3 27.5 1.0
N A:ASP10 4.3 29.8 1.0
N A:GLY11 4.3 34.5 1.0
CG A:ASP10 4.3 29.8 1.0
CB A:ASP170 4.4 32.8 1.0
CB A:PHD8 4.4 27.9 1.0
CA A:GLY11 4.5 33.8 1.0
N A:ASP170 4.6 35.8 1.0
CD A:GLU169 4.7 39.0 1.0
OE2 A:GLU169 4.9 41.4 1.0
C A:LEU9 5.0 28.3 1.0

Magnesium binding site 2 out of 2 in 6h91

Go back to Magnesium Binding Sites List in 6h91
Magnesium binding site 2 out of 2 in the Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.4 A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.4 A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg301

b:28.6
occ:1.00
O B:HOH416 2.0 22.9 1.0
OD1 B:ASP170 2.0 31.3 1.0
OD2 B:PHD8 2.0 24.0 1.0
O B:HOH413 2.1 26.7 1.0
O B:ASP10 2.1 30.6 1.0
OP2 B:PHD8 2.1 22.1 1.0
CG B:ASP170 3.0 31.9 1.0
CG B:PHD8 3.1 24.4 1.0
C B:ASP10 3.3 30.9 1.0
OD2 B:ASP170 3.4 31.2 1.0
P B:PHD8 3.4 24.1 1.0
OD1 B:PHD8 3.5 23.2 1.0
OE1 B:GLU169 3.9 33.9 1.0
CB B:ASP10 4.0 31.6 1.0
CA B:ASP10 4.1 30.2 1.0
OP1 B:PHD8 4.2 24.1 1.0
OD2 B:ASP10 4.2 36.1 1.0
N B:GLY11 4.3 29.4 1.0
N B:ASP10 4.3 29.6 1.0
CB B:ASP170 4.3 32.7 1.0
CB B:PHD8 4.4 25.6 1.0
OP3 B:PHD8 4.4 22.8 1.0
CG B:ASP10 4.4 34.9 1.0
O B:HOH404 4.4 32.1 1.0
N B:ASP170 4.5 31.5 1.0
CA B:GLY11 4.5 28.1 1.0
CD B:GLU169 4.6 32.5 1.0
OE2 B:GLU169 4.8 30.6 1.0
CA B:ASP170 4.8 32.0 1.0
C B:LEU9 4.9 28.5 1.0
OG B:SER171 5.0 28.0 1.0
CB B:SER171 5.0 27.2 1.0
N B:SER171 5.0 30.0 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 Jan 25 08:44:16 2021

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