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Atomistry » Magnesium » PDB 2wb4-2wkk » 2wfa » |
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:
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:
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 2wfaGo back to![]() ![]()
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
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.
Page generated: Wed Aug 14 06:05:53 2024
ISSN: ISSN 0027-8424 PubMed: 22505741 DOI: 10.1073/PNAS.1116855109 |
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