Atomistry » Magnesium » PDB 4c30-4cgk » 4c4s
Atomistry »
  Magnesium »
    PDB 4c30-4cgk »
      4c4s »

Magnesium in PDB 4c4s: Structure of Beta-Phosphoglucomutase in Complex with An Alpha-Fluorophosphonate Analogue of Beta-Glucose-1-Phosphate and Magnesium Trifluoride

Enzymatic activity of Structure of Beta-Phosphoglucomutase in Complex with An Alpha-Fluorophosphonate Analogue of Beta-Glucose-1-Phosphate and Magnesium Trifluoride

All present enzymatic activity of Structure of Beta-Phosphoglucomutase in Complex with An Alpha-Fluorophosphonate Analogue of Beta-Glucose-1-Phosphate and Magnesium Trifluoride:
5.4.2.6;

Protein crystallography data

The structure of Structure of Beta-Phosphoglucomutase in Complex with An Alpha-Fluorophosphonate Analogue of Beta-Glucose-1-Phosphate and Magnesium Trifluoride, PDB code: 4c4s 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) 37.634 / 1.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 37.541, 54.337, 104.346, 90.00, 90.00, 90.00
R / Rfree (%) 17.25 / 19.84

Other elements in 4c4s:

The structure of Structure of Beta-Phosphoglucomutase in Complex with An Alpha-Fluorophosphonate Analogue of Beta-Glucose-1-Phosphate and Magnesium Trifluoride also contains other interesting chemical elements:

Fluorine (F) 4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Beta-Phosphoglucomutase in Complex with An Alpha-Fluorophosphonate Analogue of Beta-Glucose-1-Phosphate and Magnesium Trifluoride (pdb code 4c4s). 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 in Complex with An Alpha-Fluorophosphonate Analogue of Beta-Glucose-1-Phosphate and Magnesium Trifluoride, PDB code: 4c4s:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 4c4s

Go back to Magnesium Binding Sites List in 4c4s
Magnesium binding site 1 out of 2 in the Structure of Beta-Phosphoglucomutase in Complex with An Alpha-Fluorophosphonate Analogue of Beta-Glucose-1-Phosphate and Magnesium Trifluoride


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 in Complex with An Alpha-Fluorophosphonate Analogue of Beta-Glucose-1-Phosphate and Magnesium Trifluoride within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1220

b:7.4
occ:1.00
 MG A:MGF1220 0.0 7.4 1.0
F3 A:MGF1220 1.8 9.6 1.0
F1 A:MGF1220 1.8 8.1 1.0
F2 A:MGF1220 1.8 9.2 1.0
OD1 A:ASP8 2.0 8.5 1.0
O6 A:GRX1219 2.2 7.3 1.0
CG A:ASP8 3.0 6.7 1.0
C6 A:GRX1219 3.1 9.4 1.0
OD2 A:ASP8 3.4 7.1 1.0
MG A:MG2833 3.4 7.4 1.0
O A:HOH2009 3.7 8.3 1.0
OG A:SER114 3.7 9.1 1.0
N A:ASP10 3.8 6.0 1.0
OD2 A:ASP10 3.9 8.1 1.0
NZ A:LYS145 3.9 8.4 1.0
N A:LEU9 4.0 6.4 1.0
N A:ALA115 4.0 8.3 1.0
CB A:ASP10 4.1 8.2 1.0
CA A:SER114 4.3 7.0 1.0
CG A:ASP10 4.3 7.2 1.0
O A:ASP10 4.4 6.3 1.0
CB A:ASP8 4.4 8.0 1.0
CB A:SER114 4.4 8.5 1.0
C5 A:GRX1219 4.5 8.0 1.0
CA A:ASP10 4.5 6.7 1.0
CA A:GLY46 4.5 8.4 1.0
O A:HOH2011 4.7 7.1 1.0
C A:LEU9 4.7 6.6 1.0
C A:SER114 4.7 9.9 1.0
CB A:ALA115 4.7 8.3 1.0
CA A:ASP8 4.7 6.5 1.0
CA A:LEU9 4.8 7.1 1.0
C A:ASP8 4.9 7.4 1.0
O5 A:GRX1219 4.9 8.5 1.0
C A:ASP10 4.9 5.5 1.0
N A:GLY46 4.9 8.2 1.0
OE2 A:GLU169 5.0 11.8 1.0
CA A:ALA115 5.0 8.3 1.0

Magnesium binding site 2 out of 2 in 4c4s

Go back to Magnesium Binding Sites List in 4c4s
Magnesium binding site 2 out of 2 in the Structure of Beta-Phosphoglucomutase in Complex with An Alpha-Fluorophosphonate Analogue of Beta-Glucose-1-Phosphate and Magnesium Trifluoride


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 in Complex with An Alpha-Fluorophosphonate Analogue of Beta-Glucose-1-Phosphate and Magnesium Trifluoride within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2833

b:7.4
occ:1.00
 F1 A:MGF1220 2.0 8.1 1.0
O A:HOH2011 2.0 7.1 1.0
OD2 A:ASP8 2.1 7.1 1.0
O A:HOH2009 2.1 8.3 1.0
OD1 A:ASP170 2.1 7.7 1.0
O A:ASP10 2.1 6.3 1.0
CG A:ASP170 3.0 8.9 1.0
CG A:ASP8 3.1 6.7 1.0
C A:ASP10 3.3 5.5 1.0
OD2 A:ASP170 3.3 8.5 1.0
OD1 A:ASP8 3.4 8.5 1.0
MG A:MGF1220 3.4 7.4 1.0
CA A:ASP10 4.0 6.7 1.0
CB A:ASP10 4.1 8.2 1.0
OE1 A:GLU169 4.1 10.3 1.0
N A:ASP10 4.1 6.0 1.0
N A:GLY11 4.3 6.2 1.0
CB A:ASP8 4.4 8.0 1.0
CB A:ASP170 4.4 8.6 1.0
O A:HOH2296 4.4 7.2 1.0
F2 A:MGF1220 4.5 9.2 1.0
N A:GLY46 4.6 8.2 1.0
N A:ASP170 4.6 6.8 1.0
CA A:GLY11 4.6 8.2 1.0
F3 A:MGF1220 4.6 9.6 1.0
O6 A:GRX1219 4.7 7.3 1.0
CB A:SER171 4.7 9.2 1.0
CD A:GLU169 4.8 9.9 1.0
C6 A:GRX1219 4.8 9.4 1.0
CA A:GLY46 4.8 8.4 1.0
CG2 A:VAL12 4.8 10.0 1.0
C A:LEU9 4.8 6.6 1.0
OE2 A:GLU169 4.9 11.8 1.0
OG A:SER171 4.9 10.6 1.0
CA A:ASP170 4.9 8.2 1.0

Reference:

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
Page generated: Thu Aug 15 16:42:08 2024

Last articles

Mg in 1YL6
Mg in 1YL5
Mg in 1YKV
Mg in 1YKQ
Mg in 1YIT
Mg in 1YIJ
Mg in 1YJF
Mg in 1YI2
Mg in 1YJ2
Mg in 1YHQ
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy