Structure of ampk bound to activator

Structure

x-ray diffraction · 3 distinct chains.

Ligands and binding sites

• AMP · Adenosine monophosphate · ligand · 2 copies · chains C
• STU · Staurosporine · ligand · chains A
• HU7 · 1-O-{6-chloro-5-[6-(dimethylamino)-2-methoxypyridin-3-yl]-1H-indole-3-carbonyl}-beta-D-glucopyranuronic acid · ligand · chains A, B
• ADP · Adenosine-5'-diphosphate · ligand · chains C
• CL · Chloride ion · ion · 4 copies · chains A
• SO4 · Sulfate ion · ion · chains C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

• 6E4U · Structure of AMPK bound to activator · the same entry in another collection · chain A against A, TM-score 1.00
• P54645 · AlphaFold monomer V2.0 prediction for 5'-AMP-activated protein kinase catalytic subunit… · a predicted model of the same protein · chain A against A, TM-score 0.99
• P80385 · AlphaFold monomer V2.0 prediction for 5'-AMP-activated protein kinase subunit gamma-1… · a predicted model of the same protein · chain C against A, TM-score 0.98
• P80386 · AlphaFold monomer V2.0 prediction for 5'-AMP-activated protein kinase subunit beta-1… · a predicted model of the same protein · chain B against A, TM-score 0.93

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P54645
• Every structure of UniProt P80386
• Every structure of UniProt P80385
• Elsewhere: RCSB PDB 6E4U · PDBe 6E4U · UniProt P54645 · UniProt P80386 · UniProt P80385