Structure of BX-795 Complexed with Unphosphorylated Human TBK1 Kinase-ULD Domain

Molecular basis of Tank-binding kinase 1 activation by transautophosphorylation.

NF-kappa-B-activating kinase, T2K, TANK-binding kinase 1

MGSQSTSNHLWLLSDILGQGATANVFRGRHKKTGDLFAIKVFNNISFLRPVDVQMREFEVLKKLNHKNIVKLFAIEEETT
TRHKVLIMEFCPCGSLYTVLEEPSNAYGLPESEFLIVLRDVVGGMNHLRENGIVHRNIKPGNIMRVIGEDGQSVYKLTDF
GAARELEDDEQFVSLYGTEEYLHPDMYERAVLRKDHQKKYGATVDLWSIGVTFYHAATGSLPFRPFEGPRRNKEVMYKII
TGKPSGAISGVQKAENGPIDWSGDMPVSCSLSRGLQVLLTPVLANILEADQEKCWGFDQFFAETSDILHRMVIHVFSLQQ
MTAHKIYIHSYNTATIFHELVYKQTKIISSNQELIYEGRRLVLEPGRLAQHFPKTTEENPIFVVSREGNSHHHHHH

0.2 M lithium sulfate, 0.1 M TRIS pH 8.5, 25% (w/v) PEG 400, VAPOR DIFFUSION, HANGING DROP, temperature 293K

THE 5-IODO SUBSTITUTION OF THE PYRIMIDINE IN BX-795 IS SENSITIVE TO RADIATION CLEAVAGE. THE IONIZED IODINE RADICALS DIFFUSE AWAY FROM ITS ORIGINAL POSITION. BOTH THE POSITIONS OF THE IODINE HAS BEEN CAPTURED AND REPRESENTED AS ALTERNATE CONFORMERS

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

Kinase, ATP Binding, Phosphorylation, TRANSFERASE-TRANSFERASE INHIBITOR complex

QSTSNHLWLLSDILGQGATANVFRGRHKKTGDLFAIKVFNNISFLRPVDVQMREFEVLKKLNHKNIVKLFAIEEETTTRH
KVLIMEFCPCGSLYTVLEEPSNAYGLPESEFLIVLRDVVGGMNHLRENGIVHRDIKPGNIMRVIGEDGQSVYKLTDFGAA
RELEDDEQFVSLYGTEEYLHPDMYERAVLRKDHQKKYGATVDLWSIGVTFYHAATGSLPFRPFEGPRRNKEVMYKIITGK
PSGAISGVQKAENGPIDWSGDMPVSCSLSRGLQVLLTPVLANILEADQEKCWGFDQFFAETSDILHRMVIHVFSLQQMTA
HKIYIHSYNTATIFHELVYKQTKIISSNQELIYEGRRLVLEPGRLAQHFPKTTEENPIFVVSRE