|
Sodium in PDB 8vme: Crystal Structure of the Gsk-3/Axin Complex Bound to A Phosphorylated Beta-Catenin T41A PeptideEnzymatic activity of Crystal Structure of the Gsk-3/Axin Complex Bound to A Phosphorylated Beta-Catenin T41A Peptide
All present enzymatic activity of Crystal Structure of the Gsk-3/Axin Complex Bound to A Phosphorylated Beta-Catenin T41A Peptide:
2.7.11.1; 2.7.11.26; Protein crystallography data
The structure of Crystal Structure of the Gsk-3/Axin Complex Bound to A Phosphorylated Beta-Catenin T41A Peptide, PDB code: 8vme
was solved by
M.D.Enos,
M.Gavagan,
N.Jameson,
J.G.Zalatan,
W.I.Weis,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 8vme:
The structure of Crystal Structure of the Gsk-3/Axin Complex Bound to A Phosphorylated Beta-Catenin T41A Peptide also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Crystal Structure of the Gsk-3/Axin Complex Bound to A Phosphorylated Beta-Catenin T41A Peptide
(pdb code 8vme). 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 Crystal Structure of the Gsk-3/Axin Complex Bound to A Phosphorylated Beta-Catenin T41A Peptide, PDB code: 8vme: Sodium binding site 1 out of 1 in 8vmeGo back to![]() ![]()
Sodium binding site 1 out
of 1 in the Crystal Structure of the Gsk-3/Axin Complex Bound to A Phosphorylated Beta-Catenin T41A Peptide
![]() Mono view ![]() Stereo pair view
Reference:
M.D.Enos,
M.Gavagan,
N.Jameson,
J.G.Zalatan,
W.I.Weis.
Structural and Functional Effects of Phosphopriming and Scaffolding in the Kinase GSK3BETA Sci.Signal. 2024.
Page generated: Wed Oct 9 14:03:30 2024
ISSN: ESSN 1937-9145 DOI: 10.1126/SCISIGNAL.ADO0881 |
Last articlesFe in 9CU2Fe in 9CU1 Fe in 9CU0 Fe in 9CJE Fe in 9CJB Fe in 9CJF Fe in 9CTZ Fe in 9CJD Fe in 9CJC Fe in 9CUF |
© Copyright 2008-2020 by atomistry.com | ||
Home | Site Map | Copyright | Contact us | Privacy |