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Magnesium in PDB 2whe: Structure of Native Beta-Phosphoglucomutase in An Open Conformation Without Bound Ligands.

Enzymatic activity of Structure of Native Beta-Phosphoglucomutase in An Open Conformation Without Bound Ligands.

All present enzymatic activity of Structure of Native Beta-Phosphoglucomutase in An Open Conformation Without Bound Ligands.:
5.4.2.6;

Protein crystallography data

The structure of Structure of Native Beta-Phosphoglucomutase in An Open Conformation Without Bound Ligands., PDB code: 2whe 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 / 1.55
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 53.239, 56.900, 75.441, 90.00, 90.00, 90.00
R / Rfree (%) 17.6 / 20.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Native Beta-Phosphoglucomutase in An Open Conformation Without Bound Ligands. (pdb code 2whe). 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 Native Beta-Phosphoglucomutase in An Open Conformation Without Bound Ligands., PDB code: 2whe:

Magnesium binding site 1 out of 1 in 2whe

Go back to Magnesium Binding Sites List in 2whe
Magnesium binding site 1 out of 1 in the Structure of Native Beta-Phosphoglucomutase in An Open Conformation Without Bound Ligands.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Native Beta-Phosphoglucomutase in An Open Conformation Without Bound Ligands. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1222

b:20.3
occ:1.00
 O A:HOH2259 2.0 34.8 1.0
OD1 A:ASP170 2.1 18.9 1.0
O A:ASP10 2.2 14.2 1.0
OD1 A:ASP8 2.3 22.7 1.0
OE1 A:GLU169 3.0 21.0 1.0
CG A:ASP170 3.2 16.8 1.0
CG A:ASP8 3.4 13.9 1.0
C A:ASP10 3.4 12.8 1.0
O A:HOH2260 3.6 27.3 1.0
O A:HOH2011 3.6 26.4 1.0
OD2 A:ASP170 3.8 16.4 1.0
CD A:GLU169 3.9 17.8 1.0
CB A:ASP8 4.0 11.9 1.0
OE2 A:GLU169 4.2 18.6 1.0
N A:GLY11 4.3 11.8 1.0
CA A:ASP10 4.3 13.1 1.0
N A:ASP170 4.3 13.2 1.0
O A:HOH2012 4.3 28.6 1.0
CA A:GLY11 4.3 12.5 1.0
CB A:ASP10 4.4 13.9 1.0
OD2 A:ASP8 4.4 17.3 1.0
CB A:ASP170 4.4 13.8 1.0
N A:ASP10 4.5 11.6 1.0
OG A:SER171 4.8 18.5 1.0
CA A:ASP170 4.8 14.8 1.0
CG2 A:VAL12 4.8 13.2 1.0
OD2 A:ASP10 4.8 25.7 1.0
N A:SER171 4.8 15.2 1.0
CB A:SER171 4.8 17.2 1.0
C A:GLY11 4.9 12.4 1.0
C A:ASP170 5.0 15.2 1.0
CG A:ASP10 5.0 19.3 1.0

Reference:

N.J.Baxter, M.W.Bowler, T.Alizadeh, M.J.Cliff, A.M.Hounslow, B.Wu, D.B.Berkowitz, N.H.Williams, G.M.Blackburn, J.P.Waltho. Atomic Details of Near-Transition State Conformers For Enzyme Phosphoryl Transfer Revealed By Mgf-3 Rather Than By Phosphoranes. Proc.Natl.Acad.Sci.Usa V. 107 4555 2010.
ISSN: ISSN 0027-8424
PubMed: 20164409
DOI: 10.1073/PNAS.0910333106
Page generated: Wed Aug 14 06:06:29 2024

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