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Atomistry » Sodium » PDB 2vrr-2wcp » 2wb5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 2vrr-2wcp » 2wb5 » |
Sodium in PDB 2wb5: Glcnacstatins Are Nanomolar Inhibitors of Human O-Glcnacase Inducing Cellular Hyper-O-GlcnacylationEnzymatic activity of Glcnacstatins Are Nanomolar Inhibitors of Human O-Glcnacase Inducing Cellular Hyper-O-Glcnacylation
All present enzymatic activity of Glcnacstatins Are Nanomolar Inhibitors of Human O-Glcnacase Inducing Cellular Hyper-O-Glcnacylation:
3.2.1.35; 3.2.1.52; Protein crystallography data
The structure of Glcnacstatins Are Nanomolar Inhibitors of Human O-Glcnacase Inducing Cellular Hyper-O-Glcnacylation, PDB code: 2wb5
was solved by
H.C.Dorfmueller,
V.S.Borodkin,
M.Schimpl,
D.M.F.Van Aalten,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2wb5:
The structure of Glcnacstatins Are Nanomolar Inhibitors of Human O-Glcnacase Inducing Cellular Hyper-O-Glcnacylation also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Glcnacstatins Are Nanomolar Inhibitors of Human O-Glcnacase Inducing Cellular Hyper-O-Glcnacylation
(pdb code 2wb5). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Glcnacstatins Are Nanomolar Inhibitors of Human O-Glcnacase Inducing Cellular Hyper-O-Glcnacylation, PDB code: 2wb5: Sodium binding site 1 out of 1 in 2wb5Go back to Sodium Binding Sites List in 2wb5
Sodium binding site 1 out
of 1 in the Glcnacstatins Are Nanomolar Inhibitors of Human O-Glcnacase Inducing Cellular Hyper-O-Glcnacylation
Mono view Stereo pair view
Reference:
H.C.Dorfmueller,
V.S.Borodkin,
M.Schimpl,
D.M.F.Van Aalten.
Glcnacstatins Are Nanomolar Inhibitors of Human O- Glcnacase Inducing Cellular Hyper-O-Glcnacylation Biochem.J. V. 420 221 2009.
Page generated: Tue Dec 15 05:57:09 2020
ISSN: ISSN 0264-6021 PubMed: 19275764 DOI: 10.1042/BJ20090110 |
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