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spinqualitylabelsall models PDB ID 1j1c Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1j1c, resolution 2.10Å ()
Ligands:	,
Activity:	Non-specific serine/threonine protein kinase, with EC number 2.7.11.1
Related:	1j1b
Structural annotation: Resources: CATH : 1J1Ca02, 1J1Ca01, 1J1Cb02, 1J1Cb01 InterPro : Ipr011009, Ipr002290, Ipr008271, Ipr000719 Pfam : PF00069 SCOP : d1j1ca_, d1j1cb_ UniProt : P49841
Functional annotation: Cellular component: cytoplasm nucleus beta-catenin destruction complex Biological process: ER overload response positive regulation of protein export from nucleus peptidyl-serine phosphorylation glycogen metabolic process protein amino acid phosphorylation Wnt receptor signaling pathway through beta-catenin intracellular signaling cascade negative regulation of apoptosis Wnt receptor signaling pathway Molecular function: nucleotide binding kinase activity transferase activity ATP binding protein binding protein serine/threonine kinase activity NF-kappaB binding glycogen synthase kinase 3 activity protein kinase activity p53 binding
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

Contents 1 Descritpion 2 Activity 3 Structure 4 External Ressources 5 References

Descritpion

Activity

at tyrosine-216 in GSK-3β or tyrosine-279 in GSK-3α enhances the enzymatic activity of GSK-3, while phosphorlyation of serine-9 in GSK-3β or serine-21 in GSK-3α significantly decreases active site availability

Structure

These are the engaged in the catalytic site of the protein, they are polar and localised in 3' end (Asp-181, Lys-183, Gln-185, Asn-186 and Ser-219. The Tau protein possesses as well as (Adenosine DiPhosphate) This enzyme is activated by phosphorylation at and inactivated by phosphorylation at Ser-9 (not shown here because this structure start at residue 35). This structure possesses 12 hydrogen bonds in order to stabilize the molecule, but in this case only three hydrogen bonds are respresented and here there is the engaged

External Ressources

References