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Magnesium in PDB 3zi4: The Structure of Beta-Phosphoglucomutase Inhibited with Glucose-6-Phospahte and Scandium Tetrafluoride

Enzymatic activity of The Structure of Beta-Phosphoglucomutase Inhibited with Glucose-6-Phospahte and Scandium Tetrafluoride

All present enzymatic activity of The Structure of Beta-Phosphoglucomutase Inhibited with Glucose-6-Phospahte and Scandium Tetrafluoride:
5.4.2.6;

Protein crystallography data

The structure of The Structure of Beta-Phosphoglucomutase Inhibited with Glucose-6-Phospahte and Scandium Tetrafluoride, PDB code: 3zi4 was solved by E.Pellegrini, M.W.Bowler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.33
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 37.152, 54.238, 104.550, 90.00, 90.00, 90.00
R / Rfree (%) 13.018 / 17.379

Other elements in 3zi4:

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

Scandium (Sc) 1 atom
Fluorine (F) 4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Structure of Beta-Phosphoglucomutase Inhibited with Glucose-6-Phospahte and Scandium Tetrafluoride (pdb code 3zi4). 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 The Structure of Beta-Phosphoglucomutase Inhibited with Glucose-6-Phospahte and Scandium Tetrafluoride, PDB code: 3zi4:

Magnesium binding site 1 out of 1 in 3zi4

Go back to Magnesium Binding Sites List in 3zi4
Magnesium binding site 1 out of 1 in the The Structure of Beta-Phosphoglucomutase Inhibited with Glucose-6-Phospahte and Scandium Tetrafluoride


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Structure of Beta-Phosphoglucomutase Inhibited with Glucose-6-Phospahte and Scandium Tetrafluoride within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1219

b:7.0
occ:1.00
 F1 A:SFL1221 2.0 6.6 1.0
OD1 A:ASP170 2.0 6.0 1.0
OD2 A:ASP8 2.0 6.8 1.0
O A:HOH2012 2.1 7.3 1.0
O A:ASP10 2.1 5.9 1.0
O A:HOH2018 2.1 6.8 1.0
CG A:ASP170 3.0 6.7 1.0
CG A:ASP8 3.1 6.2 1.0
C A:ASP10 3.3 5.7 1.0
OD2 A:ASP170 3.4 7.7 1.0
OD1 A:ASP8 3.5 6.5 1.0
SC A:SFL1221 3.5 7.7 0.8
F4 A:SFL1221 3.7 14.6 1.0
O2 A:BG61220 3.9 7.4 1.0
CA A:ASP10 4.0 5.6 1.0
OE1 A:GLU169 4.0 11.1 1.0
N A:ASP10 4.1 6.2 1.0
CB A:ASP10 4.1 5.7 1.0
N A:GLY11 4.3 6.0 1.0
CB A:ASP170 4.4 6.5 1.0
CB A:ASP8 4.4 6.7 1.0
F3 A:SFL1221 4.5 7.6 1.0
N A:ASP170 4.5 6.9 1.0
CA A:GLY11 4.6 6.5 1.0
O A:HOH2422 4.6 8.7 1.0
CB A:SER171 4.7 8.0 1.0
CD A:GLU169 4.7 9.5 1.0
OG A:SER171 4.7 8.7 1.0
O1 A:BG61220 4.8 6.6 1.0
N A:GLY46 4.8 7.5 1.0
C A:LEU9 4.8 5.4 1.0
OE2 A:GLU169 4.9 10.6 1.0
CA A:ASP170 4.9 6.1 1.0
CG2 A:VAL12 4.9 8.2 1.0
C A:GLY11 5.0 7.7 1.0
N A:SER171 5.0 7.2 1.0

Reference:

M.W.Bowler, E.Pellegrini. Metal Fluorides: Multi-Functional Tools For the Study of Phosphoryl Transfer Enzymes To Be Published.
Page generated: Mon Aug 11 05:14:10 2025

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