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Magnesium in PDB 5ok2: Structure of the D10N Mutant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited with Glucose 6-Phosphate and Tetrafluoroaluminate to 1.1A Resolution.

Enzymatic activity of Structure of the D10N Mutant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited with Glucose 6-Phosphate and Tetrafluoroaluminate to 1.1A Resolution.

All present enzymatic activity of Structure of the D10N Mutant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited with Glucose 6-Phosphate and Tetrafluoroaluminate to 1.1A Resolution.:
5.4.2.6;

Protein crystallography data

The structure of Structure of the D10N Mutant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited with Glucose 6-Phosphate and Tetrafluoroaluminate to 1.1A Resolution., PDB code: 5ok2 was solved by A.J.Robertson, C.Bisson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 52.39 / 1.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 37.540, 54.280, 104.670, 90.00, 90.00, 90.00
R / Rfree (%) 14.8 / 17

Other elements in 5ok2:

The structure of Structure of the D10N Mutant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited with Glucose 6-Phosphate and Tetrafluoroaluminate to 1.1A Resolution. also contains other interesting chemical elements:

Fluorine (F) 4 atoms
Aluminium (Al) 1 atom
Sodium (Na) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of the D10N Mutant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited with Glucose 6-Phosphate and Tetrafluoroaluminate to 1.1A Resolution. (pdb code 5ok2). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of the D10N Mutant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited with Glucose 6-Phosphate and Tetrafluoroaluminate to 1.1A Resolution., PDB code: 5ok2:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 5ok2

Go back to Magnesium Binding Sites List in 5ok2
Magnesium binding site 1 out of 2 in the Structure of the D10N Mutant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited with Glucose 6-Phosphate and Tetrafluoroaluminate to 1.1A Resolution.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the D10N Mutant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited with Glucose 6-Phosphate and Tetrafluoroaluminate to 1.1A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg308

b:8.1
occ:1.00
 F1 A:ALF301 2.0 8.2 1.0
OD2 A:ASP8 2.0 8.6 1.0
OD1 A:ASP170 2.0 8.5 1.0
O A:HOH431 2.1 9.5 1.0
O A:ASN10 2.1 8.5 1.0
O A:HOH463 2.1 9.3 1.0
CG A:ASP8 3.0 8.2 1.0
CG A:ASP170 3.0 8.6 1.0
C A:ASN10 3.3 7.4 1.0
OD2 A:ASP170 3.4 9.3 1.0
OD1 A:ASP8 3.4 8.4 1.0
AL A:ALF301 3.5 8.2 1.0
F2 A:ALF301 3.6 8.9 1.0
O2 A:BG6310 3.8 8.8 1.0
CA A:ASN10 4.0 7.9 1.0
OE1 A:GLU169 4.0 11.9 1.0
N A:ASN10 4.0 7.7 1.0
CB A:ASN10 4.1 8.1 1.0
F4 A:ALF301 4.2 8.4 1.0
N A:GLY11 4.3 7.7 1.0
CB A:ASP8 4.3 8.2 1.0
CB A:ASP170 4.4 8.8 1.0
N A:ASP170 4.5 8.8 1.0
O1 A:BG6310 4.6 8.3 1.0
CA A:GLY11 4.6 8.7 1.0
O A:HOH537 4.6 10.3 1.0
C A:LEU9 4.8 7.0 0.5
CG2 A:VAL12 4.8 10.0 1.0
C A:LEU9 4.8 7.4 0.5
CB A:SER171 4.8 10.4 1.0
CD A:GLU169 4.8 11.1 1.0
CA A:ASP170 4.9 8.9 1.0
N A:GLY46 4.9 9.5 1.0
OG A:SER171 4.9 11.1 1.0
C A:GLY11 5.0 9.3 1.0
C2 A:BG6310 5.0 8.7 1.0
N A:SER171 5.0 9.4 1.0

Magnesium binding site 2 out of 2 in 5ok2

Go back to Magnesium Binding Sites List in 5ok2
Magnesium binding site 2 out of 2 in the Structure of the D10N Mutant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited with Glucose 6-Phosphate and Tetrafluoroaluminate to 1.1A Resolution.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of the D10N Mutant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited with Glucose 6-Phosphate and Tetrafluoroaluminate to 1.1A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg309

b:16.9
occ:0.50
 O A:HOH428 2.1 27.4 1.0
O A:HOH630 2.1 25.2 0.5
O A:HOH633 2.1 23.8 0.5
O A:HOH597 2.1 24.8 1.0
O A:HOH642 2.1 20.0 0.5
O A:THR129 4.2 11.3 1.0
CA A:GLY130 4.2 11.8 1.0
O A:HOH401 4.3 26.2 1.0
CG2 A:THR129 4.6 14.4 1.0
C A:THR129 4.6 10.0 1.0
O A:HOH598 4.6 40.4 1.0
N A:GLY130 4.6 10.6 1.0
O A:PHE132 4.8 14.7 1.0
C A:GLY130 4.9 12.3 1.0

Reference:

L.A.Johnson, A.J.Robertson, N.J.Baxter, C.R.Trevitt, C.Bisson, Y.Jin, H.P.Wood, A.M.Hounslow, M.J.Cliff, G.M.Blackburn, M.W.Bowler, J.P.Waltho. Van Der Waals Contact Between Nucleophile and Transferring Phosphorus Is Insufficient to Achieve Enzyme Transition-State Architecture Acs Catalysis 2018.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.8B01612
Page generated: Mon Sep 30 01:01:44 2024

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