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Magnesium in PDB 2wfa: Structure of Beta-Phosphoglucomutase Inhibited with Beryllium Trifluoride, in An Open Conformation.

Enzymatic activity of Structure of Beta-Phosphoglucomutase Inhibited with Beryllium Trifluoride, in An Open Conformation.

All present enzymatic activity of Structure of Beta-Phosphoglucomutase Inhibited with Beryllium Trifluoride, in An Open Conformation.:
5.4.2.6;

Protein crystallography data

The structure of Structure of Beta-Phosphoglucomutase Inhibited with Beryllium Trifluoride, in An Open Conformation., PDB code: 2wfa 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 / 1.65
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 53.300, 57.300, 75.000, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 23.7

Other elements in 2wfa:

The structure of Structure of Beta-Phosphoglucomutase Inhibited with Beryllium Trifluoride, in An Open Conformation. also contains other interesting chemical elements:

Fluorine (F) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Beta-Phosphoglucomutase Inhibited with Beryllium Trifluoride, in An Open Conformation. (pdb code 2wfa). 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 Structure of Beta-Phosphoglucomutase Inhibited with Beryllium Trifluoride, in An Open Conformation., PDB code: 2wfa:

Magnesium binding site 1 out of 1 in 2wfa

Go back to Magnesium Binding Sites List in 2wfa
Magnesium binding site 1 out of 1 in the Structure of Beta-Phosphoglucomutase Inhibited with Beryllium Trifluoride, in An Open Conformation.


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 Beryllium Trifluoride, in An Open Conformation. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1222

b:11.8
occ:1.00
 F3 A:BEF1223 2.0 13.6 1.0
OD1 A:ASP8 2.0 9.0 1.0
O A:ASP10 2.0 12.3 1.0
OD1 A:ASP170 2.0 11.4 1.0
O A:HOH2152 2.1 14.9 1.0
O A:HOH2154 2.2 12.4 1.0
CG A:ASP170 3.0 12.4 1.0
CG A:ASP8 3.1 10.2 1.0
C A:ASP10 3.2 12.4 1.0
BE A:BEF1223 3.2 13.2 1.0
OD2 A:ASP170 3.3 11.4 1.0
OD2 A:ASP8 3.4 10.4 1.0
OE1 A:GLU169 3.9 13.5 1.0
CA A:ASP10 4.0 12.7 1.0
CB A:ASP10 4.0 13.2 1.0
N A:ASP10 4.1 12.4 1.0
N A:GLY11 4.2 12.3 1.0
F2 A:BEF1223 4.3 12.8 1.0
F1 A:BEF1223 4.3 12.5 1.0
OD2 A:ASP10 4.3 19.9 1.0
CB A:ASP170 4.3 11.4 1.0
O A:HOH2139 4.3 24.8 1.0
CB A:ASP8 4.4 10.1 1.0
CA A:GLY11 4.5 12.5 1.0
N A:ASP170 4.5 10.9 1.0
CD A:GLU169 4.6 13.7 1.0
CG A:ASP10 4.6 16.0 1.0
OE2 A:GLU169 4.7 13.1 1.0
CA A:ASP170 4.9 11.4 1.0
N A:SER171 4.9 11.7 1.0
C A:LEU9 4.9 11.8 1.0
CB A:SER171 4.9 12.8 1.0

Reference:

J.L.Griffin, M.W.Bowler, N.J.Baxter, K.N.Leigh, H.R.Dannatt, A.M.Hounslow, G.M.Blackburn, C.E.Webster, M.J.Cliff, J.P.Waltho. Near Attack Conformers Dominate Beta-Phosphoglucomutase Complexes Where Geometry and Charge Distribution Reflect Those of Substrate. Proc.Natl.Acad.Sci.Usa V. 109 6910 2012.
ISSN: ISSN 0027-8424
PubMed: 22505741
DOI: 10.1073/PNAS.1116855109
Page generated: Wed Aug 14 06:05:53 2024

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