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Magnesium in PDB 5o6r: Structure of Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1-Phosphate and Aluminium Tetrafluoride

Enzymatic activity of Structure of Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1-Phosphate and Aluminium Tetrafluoride

All present enzymatic activity of Structure of Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1-Phosphate and Aluminium Tetrafluoride:
5.4.2.6;

Protein crystallography data

The structure of Structure of Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1-Phosphate and Aluminium Tetrafluoride, PDB code: 5o6r was solved by M.W.Bowler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.36
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 36.300, 54.900, 107.560, 90.00, 90.00, 90.00
R / Rfree (%) 11.5 / 14.9

Other elements in 5o6r:

The structure of Structure of Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1-Phosphate and Aluminium Tetrafluoride also contains other interesting chemical elements:

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

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1-Phosphate and Aluminium Tetrafluoride (pdb code 5o6r). 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 Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1-Phosphate and Aluminium Tetrafluoride, PDB code: 5o6r:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 5o6r

Go back to Magnesium Binding Sites List in 5o6r
Magnesium binding site 1 out of 2 in the Structure of Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1-Phosphate and Aluminium Tetrafluoride


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1-Phosphate and Aluminium Tetrafluoride within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg301

b:8.2
occ:1.00
 F2 A:ALF303 2.0 6.3 0.8
OD2 A:ASP8 2.0 6.9 1.0
O A:ASN10 2.1 8.2 1.0
OD1 A:ASP170 2.1 8.4 1.0
O A:HOH576 2.1 9.5 1.0
O A:HOH443 2.1 9.5 1.0
CG A:ASP8 3.1 6.8 1.0
CG A:ASP170 3.1 8.4 1.0
C A:ASN10 3.2 6.7 1.0
OD1 A:ASP8 3.5 6.8 1.0
AL A:ALF303 3.5 6.7 0.8
F4 A:ALF303 3.5 8.7 0.8
OD2 A:ASP170 3.5 10.7 1.0
O A:HOH656 3.9 11.1 1.0
OE1 A:GLU169 3.9 10.4 1.0
CA A:ASN10 4.0 6.9 1.0
N A:ASN10 4.1 6.2 1.0
CB A:ASN10 4.2 7.1 1.0
N A:GLY11 4.3 7.1 1.0
F3 A:ALF303 4.3 7.0 0.8
O A:HOH505 4.3 25.2 1.0
O A:HOH407 4.4 10.1 1.0
CB A:ASP170 4.4 7.2 1.0
CB A:ASP8 4.4 6.4 1.0
N A:ASP170 4.5 7.0 1.0
CA A:GLY11 4.5 7.6 1.0
CD A:GLU169 4.7 9.1 1.0
CB A:SER171 4.7 10.3 1.0
OG A:SER171 4.8 12.5 1.0
OE2 A:GLU169 4.8 10.4 1.0
CA A:ASP170 4.8 7.4 1.0
N A:SER171 4.9 8.0 1.0
C A:LEU9 4.9 6.6 1.0
C A:ASP170 5.0 8.1 1.0

Magnesium binding site 2 out of 2 in 5o6r

Go back to Magnesium Binding Sites List in 5o6r
Magnesium binding site 2 out of 2 in the Structure of Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1-Phosphate and Aluminium Tetrafluoride


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1-Phosphate and Aluminium Tetrafluoride within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg304

b:24.6
occ:1.00
 O A:HOH555 1.9 20.5 1.0
O A:HOH530 2.0 27.4 1.0
O A:HOH723 2.1 27.3 1.0
O A:HOH634 2.1 19.9 1.0
O A:HOH737 3.0 25.0 1.0
O A:HOH473 3.3 32.5 1.0
O A:HOH497 3.9 19.5 1.0
O A:HOH444 4.2 14.9 1.0
O A:VAL188 4.3 9.8 1.0
O A:HOH718 4.4 39.8 1.0
O A:ASP170 4.4 10.3 1.0
OD2 A:ASP170 4.5 10.7 1.0
CA A:GLY189 4.5 10.0 1.0
CB A:ASP170 4.6 7.2 1.0
O A:HOH498 4.7 21.6 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 00:12:38 2024

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