Changes

* GSK3 has the typical two-domain kinase fold with a beta-strand domain (residues 25−138) at the N-terminal end and an alpha-helical domain at the C-terminal end (residues 139−343). <br>* The ATP-binding site is at the interface of the alpha-helical and beta-strand domain and is bordered by the glycine-rich loop and the hinge. <br>* The activation loop (residues 200−226) runs along the surface of the substrate binding groove. <br>* The C-terminal 39 residues (residues 344−382) are outside the core kinase fold and form a small domain that packs against the alpha-helical domain. <br>[[image:gsk3_2.jpg|right|300 px]]* The beta-strand domain consists of seven antiparallel beta-strands: strands 2−6 form a -barrel that is interrupted between strand 4 and 5 by a short helix (residue 96−102) that packs against the beta-barrel. <br>* This helix is conserved in all kinases, and two of its residues play key roles in the catalytic activity of the enzyme. Arg 96 is involved in the alignment of the two domains. Glu 97 is positioned in the active site and forms a salt bridge with Lys 85, a key residue in catalysis.<br>* Molecular weight: 46744.3 <br>* Theoretical pI: 8.98 <br>* Total number of negatively charged residues (Asp + Glu): 41 <br>* Total number of positively charged residues (Arg + Lys): 50 <br>

'''Atomic composition:'''  ** Carbon C 2085 <br>** Hydrogen H 3285 <br>** Nitrogen N 575 <br>** Oxygen O 618 <br>** Sulfur S 14 <br>* Formula: C2085H3285N575O618S14 * Total number of atoms: 6577  '''Prediction search done on NetPhos 2.0 server for GSK3''' Prediction search done on NetPhos 2.0 server, which produces neural network predictions for serine, threonine and tyrosine phosphorylation sites in eukaryotic proteins. [[image:gsk3_2predication-gsk3.jpg|center|300 px]]