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Atomistry » Aluminium » PDB 1vfx-2x2f » 2wf7 » |
Aluminium in PDB 2wf7: Structure of Beta-Phosphoglucomutase Inhibited with Glucose- 6-Phosphonate and Aluminium TetrafluorideEnzymatic activity of Structure of Beta-Phosphoglucomutase Inhibited with Glucose- 6-Phosphonate and Aluminium Tetrafluoride
All present enzymatic activity of Structure of Beta-Phosphoglucomutase Inhibited with Glucose- 6-Phosphonate and Aluminium Tetrafluoride:
5.4.2.6; Protein crystallography data
The structure of Structure of Beta-Phosphoglucomutase Inhibited with Glucose- 6-Phosphonate and Aluminium Tetrafluoride, PDB code: 2wf7
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 2wf7:
The structure of Structure of Beta-Phosphoglucomutase Inhibited with Glucose- 6-Phosphonate and Aluminium Tetrafluoride also contains other interesting chemical elements:
Aluminium Binding Sites:
The binding sites of Aluminium atom in the Structure of Beta-Phosphoglucomutase Inhibited with Glucose- 6-Phosphonate and Aluminium Tetrafluoride
(pdb code 2wf7). This binding sites where shown within
5.0 Angstroms radius around Aluminium atom.
In total only one binding site of Aluminium was determined in the Structure of Beta-Phosphoglucomutase Inhibited with Glucose- 6-Phosphonate and Aluminium Tetrafluoride, PDB code: 2wf7: Aluminium binding site 1 out of 1 in 2wf7Go back to Aluminium Binding Sites List in 2wf7
Aluminium binding site 1 out
of 1 in the Structure of Beta-Phosphoglucomutase Inhibited with Glucose- 6-Phosphonate and Aluminium Tetrafluoride
Mono view Stereo pair view
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.
Page generated: Wed Jul 10 09:32:58 2024
ISSN: ISSN 0027-8424 PubMed: 25104750 DOI: 10.1073/PNAS.1402850111 |
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