Human AMP-activated protein kinase alpha 2 subunit kinase domain (T172D) complexed with compound C

RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Structural basis for compound C inhibition of the human AMP-activated protein kinase alpha 2 subunit kinase domain

5'-AMP-activated protein kinase catalytic subunit alpha-2

GSKHDGRVKIGHYVLGDTLGVGTFGKVKIGEHQLTGHKVAVKILNRQKIRSLDVVGKIKREIQNLKLFRHPHIIKLYQVI
STPTDFFMVMEYVSGGELFDYICKHGRVEEMEARRLFQQILSAVDYCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNM
MSDGEFLRDSCGSPNYAAPEVISGRLYAGPEVDIWSCGVILYALLCGTLPFDDEHVPTLFKKIRGGVFYIPEYLNRSVAT
LLMHMLQVDPLKRATIKDIREHEWFKQDLPSYLFPE

0.1M Bis-Tris (pH 6.5), 1.5M ammonium sulfate, 0.1M NaCl, 0.5mM Compound C, 5mM MgCl2, VAPOR DIFFUSION, SITTING DROP, temperature 293K

RIKEN Structural Genomics/Proteomics Initiative

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

Structural Genomics, RIKEN Structural Genomics/Proteomics Initiative, RSGI, Transferase, Signaling protein, Serine/threonine protein kinase, Phosphorylation, ATP-binding, Nucleotide-binding, Cholesterol biosynthesis, Fatty acid biosynthesis, Lipid synthesis, glucose metabolism, Magnesium, Metal-binding, Serine/threonine-protein kinase, Steroid biosynthesis, TRANSFERASE-TRANSFERASE INHIBITOR complex

KHDGRVKIGHYVLGDTLGVGTFGKVKIGEHQLTGHKVAVKILNRQKIRSLDVVGKIKREIQNLKLFRHPHIIKLYQVIST
PTDFFMVMEYVSGGELFDYICKHGRVEEMEARRLFQQILSAVDYCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMS
DGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSCGVILYALLCGTLPFDDEHVPTLFKKIRGGVFYIPEYLNRSVATLL
MHMLQVDPLKRATIKDIREHEWFKQDLPSYLFPE