Magnesium in PDB 6h92: Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.6 A

Enzymatic activity of Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.6 A

All present enzymatic activity of Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.6 A:
5.4.2.6;

Protein crystallography data

The structure of Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.6 A, PDB code: 6h92 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) 47.82 / 2.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 38.410, 117.180, 52.980, 90.00, 98.66, 90.00
R / Rfree (%) 23.3 / 31.6

Other elements in 6h92:

The structure of Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.6 A also contains other interesting chemical elements:

Sodium (Na) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.6 A (pdb code 6h92). 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 Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.6 A, PDB code: 6h92:

Magnesium binding site 1 out of 1 in 6h92

Go back to Magnesium Binding Sites List in 6h92
Magnesium binding site 1 out of 1 in the Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.6 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 2.6 A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg301

b:31.1
occ:1.00
OD1 A:ASP170 1.9 39.0 1.0
OP1 A:PHD8 2.3 27.3 1.0
OD2 A:PHD8 2.3 32.3 1.0
O A:ASP10 2.3 30.8 1.0
CG A:ASP170 2.9 37.6 1.0
OD2 A:ASP170 3.2 38.6 1.0
CG A:PHD8 3.4 31.2 1.0
C A:ASP10 3.5 31.3 1.0
P A:PHD8 3.7 30.4 1.0
OE1 A:GLU169 3.7 46.8 1.0
OD1 A:PHD8 3.9 30.4 1.0
OG A:SER171 4.1 36.0 1.0
CB A:ASP10 4.2 33.7 1.0
CB A:ASP170 4.3 36.6 1.0
OD2 A:ASP10 4.3 34.1 1.0
CA A:ASP10 4.3 32.0 1.0
N A:ASP170 4.5 36.0 1.0
N A:GLY11 4.5 30.1 1.0
O A:HOH403 4.5 14.7 1.0
N A:ASP10 4.6 32.2 1.0
CB A:PHD8 4.6 31.3 1.0
OP3 A:PHD8 4.6 30.1 1.0
OP2 A:PHD8 4.6 29.8 1.0
CG A:ASP10 4.7 34.7 1.0
CD A:GLU169 4.7 42.6 1.0
CB A:SER171 4.7 36.1 1.0
CA A:GLY11 4.7 29.5 1.0
CA A:ASP170 4.8 36.1 1.0
N A:SER171 4.8 37.0 1.0
C A:ASP170 4.9 35.7 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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