Magnesium in PDB 2wf7: Structure of Beta-Phosphoglucomutase Inhibited with Glucose- 6-Phosphonate and Aluminium Tetrafluoride

All present enzymatic activity of Structure of Beta-Phosphoglucomutase Inhibited with Glucose- 6-Phosphonate and Aluminium Tetrafluoride:
5.4.2.6;

The structure of Structure of Beta-Phosphoglucomutase Inhibited with Glucose- 6-Phosphonate and Aluminium Tetrafluoride, PDB code: 2wf7 was solved by M.W.Bowler, N.J.Baxter, C.E.Webster, S.Pollard, T.Alizadeh, A.M.Hounslow, M.J.Cliff, W.Bermel, N.H.Williams, F.Hollfelder, G.M.Blackburn, J.P.Waltho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.05
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	37.500, 54.300, 104.700, 90.00, 90.00, 90.00
R / Rfree (%)	15.3 / 17.6

The structure of Structure of Beta-Phosphoglucomutase Inhibited with Glucose- 6-Phosphonate and Aluminium Tetrafluoride also contains other interesting chemical elements:

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

The binding sites of Magnesium atom in the Structure of Beta-Phosphoglucomutase Inhibited with Glucose- 6-Phosphonate and Aluminium Tetrafluoride (pdb code 2wf7). 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 Inhibited with Glucose- 6-Phosphonate and Aluminium Tetrafluoride, PDB code: 2wf7:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of Beta-Phosphoglucomutase Inhibited with Glucose- 6-Phosphonate 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 Inhibited with Glucose- 6-Phosphonate and Aluminium Tetrafluoride within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1220 b:6.0 occ:1.00 F4 A:ALF1219 2.0 6.3 1.0 OD1 A:ASP170 2.0 6.5 1.0 OD2 A:ASP8 2.1 6.6 1.0 O A:ASP10 2.1 6.3 1.0 O A:HOH2240 2.1 7.6 1.0 O A:HOH2241 2.1 7.4 1.0 CG A:ASP170 3.0 6.0 1.0 CG A:ASP8 3.0 6.2 1.0 C A:ASP10 3.2 5.7 1.0 OD2 A:ASP170 3.3 6.9 1.0 OD1 A:ASP8 3.4 6.6 1.0 AL A:ALF1219 3.5 6.3 1.0 F3 A:ALF1219 3.6 7.0 1.0 O2 A:G7P1221 3.8 6.8 1.0 CA A:ASP10 4.0 5.6 1.0 OE1 A:GLU169 4.0 9.3 1.0 N A:ASP10 4.0 5.7 1.0 CB A:ASP10 4.1 5.8 1.0 F2 A:ALF1219 4.3 6.5 1.0 N A:GLY11 4.3 5.7 1.0 CB A:ASP170 4.3 6.7 1.0 CB A:ASP8 4.4 6.6 1.0 N A:ASP170 4.5 6.5 1.0 CA A:GLY11 4.5 5.9 1.0 O1 A:G7P1221 4.6 6.3 1.0 O A:HOH2283 4.6 8.4 1.0 CD A:GLU169 4.8 8.5 1.0 C A:LEU9 4.8 5.5 1.0 CG2 A:VAL12 4.8 7.9 1.0 CB A:SER171 4.8 8.3 1.0 CA A:ASP170 4.9 6.8 1.0 C A:GLY11 4.9 6.0 1.0 C2 A:G7P1221 4.9 6.8 1.0 N A:SER171 4.9 7.5 1.0 OG A:SER171 5.0 9.5 1.0 N A:GLY46 5.0 8.2 1.0 OE2 A:GLU169 5.0 9.8 1.0

Magnesium binding site 2 out of 2 in the Structure of Beta-Phosphoglucomutase Inhibited with Glucose- 6-Phosphonate 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 Inhibited with Glucose- 6-Phosphonate and Aluminium Tetrafluoride within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg2801 b:12.2 occ:0.70 O A:HOH2205 2.1 15.0 1.0 O A:HOH2080 2.1 19.7 1.0 O A:HOH2206 2.1 14.2 1.0 O A:HOH2209 4.0 25.4 1.0 CA A:GLY130 4.2 8.9 1.0 O A:THR129 4.2 8.8 1.0 O A:HOH2197 4.2 24.1 1.0 O A:HOH2207 4.3 13.1 1.0 O A:HOH2083 4.6 27.8 1.0 C A:THR129 4.6 8.1 1.0 CG2 A:THR129 4.6 11.5 1.0 N A:GLY130 4.7 8.4 1.0 O A:PHE132 4.7 10.9 1.0 O A:HOH2210 4.8 28.6 1.0 C A:GLY130 5.0 9.0 1.0

Y.Jin, D.Bhattasali, E.Pellegrini, S.M.Forget, N.J.Baxter, M.J.Cliff, M.W.Bowler, D.L.Jakeman, G.M.Blackburn, J.P.Waltho. Alpha-Fluorophosphonates Reveal How A Phosphomutase Conserves Transition State Conformation Over Hexose Recognition in Its Two-Step Reaction. Proc.Natl.Acad.Sci.Usa V. 111 12384 2014.
ISSN: ISSN 0027-8424
PubMed: 25104750
DOI: 10.1073/PNAS.1402850111