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Magnesium in PDB 8q1d: D10N Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in Complex with Fructose 1,6-Bisphosphate

Enzymatic activity of D10N Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in Complex with Fructose 1,6-Bisphosphate

All present enzymatic activity of D10N Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in Complex with Fructose 1,6-Bisphosphate:
5.4.2.6;

Protein crystallography data

The structure of D10N Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in Complex with Fructose 1,6-Bisphosphate, PDB code: 8q1d was solved by F.A.Cruz-Navarrete, N.J.Baxter, A.J.Flinders, A.Buzoianu, M.J.Cliff, P.J.Baker, J.P.Waltho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 54.43 / 1.75
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 31.888, 71.382, 83.909, 90, 90, 90
R / Rfree (%) 16.1 / 25.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the D10N Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in Complex with Fructose 1,6-Bisphosphate (pdb code 8q1d). 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 D10N Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in Complex with Fructose 1,6-Bisphosphate, PDB code: 8q1d:

Magnesium binding site 1 out of 1 in 8q1d

Go back to Magnesium Binding Sites List in 8q1d
Magnesium binding site 1 out of 1 in the D10N Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in Complex with Fructose 1,6-Bisphosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of D10N Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in Complex with Fructose 1,6-Bisphosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg302

b:53.0
occ:1.00
 OD1 A:ASP170 2.1 27.3 1.0
O A:HOH410 2.2 25.0 1.0
O A:HOH522 2.3 47.0 1.0
O5P A:FBP301 2.3 19.9 1.0
OD2 A:ASP8 2.4 31.6 1.0
O A:ASN10 2.5 20.1 1.0
CG A:ASP170 2.9 37.9 1.0
OD2 A:ASP170 3.0 31.7 1.0
CG A:ASP8 3.5 30.9 1.0
C A:ASN10 3.6 27.8 1.0
OE2 A:GLU169 3.8 22.4 1.0
P2 A:FBP301 3.9 21.6 1.0
O A:HOH450 4.0 35.2 1.0
OD1 A:ASP8 4.0 30.0 1.0
OG A:SER171 4.3 22.3 1.0
CB A:ASP170 4.4 26.4 1.0
O A:HOH530 4.4 27.0 1.0
CB A:ASN10 4.4 26.4 1.0
CA A:ASN10 4.5 19.3 1.0
O4P A:FBP301 4.5 22.1 1.0
O A:HOH561 4.6 48.3 1.0
CB A:SER171 4.6 25.1 1.0
N A:GLY11 4.6 19.9 1.0
N A:ASN10 4.6 15.9 1.0
CA A:GLY11 4.7 22.5 1.0
O6P A:FBP301 4.7 20.1 1.0
CD A:GLU169 4.7 38.9 1.0
O6 A:FBP301 4.7 22.6 1.0
CB A:ASP8 4.7 23.6 1.0
C6 A:FBP301 4.7 23.1 1.0
O A:HOH475 4.8 52.7 1.0
OE1 A:GLU169 4.9 24.4 1.0
N A:SER171 4.9 22.9 1.0
N A:ASP170 5.0 21.5 1.0

Reference:

F.A.Cruz-Navarrete, N.J.Baxter, A.J.Flinders, A.Buzoianu, M.J.Cliff, P.J.Baker, J.P.Waltho. Peri Active Site Catalysis of Proline Isomerisation Is the Molecular Basis of Allomorphy in Beta-Phosphoglucomutase. Commun Biol V. 7 909 2024.
ISSN: ESSN 2399-3642
PubMed: 39068257
DOI: 10.1038/S42003-024-06577-9
Page generated: Fri Oct 4 16:29:10 2024

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