6RST: TBK1

TBK1 in complex with inhibitor compound 24. Determined by X-ray diffraction at 3.29 Å resolution. Released 1 Jan 2020.

Method: X-ray diffraction
Resolution: 3.29 Å
Organism: Homo sapiens
Chains: 1
Atoms: 5,106
Mol. weight: 76.72 kDa
Ligands: KHQ
Released: 1 Jan 2020

Explore 6RST in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6RST contains 22 α-helices and 22 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 22 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	3	1	1
β-strand	4	1	2
β-strand	7-18	12	1
β-strand	21-28	8	1
β-strand	34-39	6	1
α-helix	49-60	12
β-strand	67	1	3
β-strand	70-75	6	1
β-strand	76	1	2
β-strand	82-87	6	1
β-strand	93	1	3
α-helix	94-98	5
α-helix	101-103	3
α-helix	109-128	20
α-helix	138-140	3
β-strand	141-145	5	3
β-strand	151-155	5	3
α-helix	177-179	3
α-helix	203-216	14
β-strand	221-222	2	4
α-helix	232-240	9
β-strand	247-250	4	4
β-strand	257-260	4	4
α-helix	271-284	14
α-helix	295-306	12
β-strand	308-315	8	5
α-helix	316-318	3
β-strand	320-327	8	5
β-strand	331	1	6
α-helix	332-343	12
β-strand	351-354	4	5
β-strand	357-359	3	5
β-strand	366	1	6
α-helix	367-369	3
β-strand	379-382	4	5
α-helix	397-399	3
α-helix	408-480	73
α-helix	493-526	34
α-helix	535-540	6
α-helix	548-572	25
α-helix	577-600	24
α-helix	601-606	6
α-helix	607-647	41
α-helix	651-653	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein kinase TBK1	A	protein	663	Homo sapiens	Q9UHD2 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6RST_1 Serine/threonine-protein kinase TBK1 (chains A)
GSGSAMGQSTSNHLWLLSDILGQGATANVFRGRHKKTGDLFAIKVFNNISFLRPVDVQMR
EFEVLKKLNHKNIVKLFAIEEETTTRHKVLIMEFCPCGSLYTVLEEPSNAYGLPESEFLI
VLRDVVGGMNHLRENGIVHRDIKPGNIMRVIGEDGQSVYKLTDFGAARELEDDEQFVSLY
GTEEYLHPDMYERAVLRKDHQKKYGATVDLWSIGVTFYHAATGSLPFRPFEGPRRNKEVM
YKIITGKPSGAISGVQKAENGPIDWSGDMPVSCSLSRGLQVLLTPVLANILEADQEKCWG
FDQFFAETSDILHRMVIHVFSLQQMTAHKIYIHSYNTATIFHELVYKQTKIISSNQELIY
EGRRLVLEPGRLAQHFPKTTEENPIFVVSREPLNTIGLIYEKISLPKVHPRYDLDGDASM
AKAITGVVCYACRIASTLLLYQELMRKGIRWLIELIKDDYNETVHKKTEVVITLDFCIRN
IEKTVKVYEKLMKINLEAAELGEISDIHTKLLRLSSSQGTIETSLQDIDSRLSPGGSLAD
AWAHQEGTHPKDRNVEKLQVLLNCMTEIYYQFKKDKAERRLAYNEEQIHKFDKQKLYYHA
TKAMTHFTDECVKKYEAFLNKSEEWIRKMLHLRKQLLSLTNQCFDIEEEVSKYQEYTNEL
QET

Ligands and cofactors

ID	Name	Formula	Copies
KHQ	1-[4-[(1~{R})-1-[2-[[5-[1-(cyclopropylmethyl)pyrazol-4-yl]-1~{H}-benzimidazol-2…	C28 H31 F3 N8 O	1

Primary citation

Discovery of BAY-985, a Highly Selective TBK1/IKK epsilon Inhibitor. Lefranc, J., Schulze, V.K., Hillig, R.C. et al. J Med Chem (2020) 63:601-612. DOI 10.1021/acs.jmedchem.9b01460 · PubMed

Other PDB entries of the same protein (UniProt Q9UHD2 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5EP6 1.45 Å, The crystal structure of NAP1 in complex with TBK1
4EFO 1.77 Å, Crystal structure of the ubiquitin-like domain of human TBK1
4EUU 1.8 Å, Structure of BX-795 Complexed with Human TBK1 Kinase Domain Phosphorylated on Ser172
5EOF 2.05 Å, Crystal structure of OPTN NTD and TBK1 CTD complex
4IM0 2.4 Å, Structure of Tank-Binding Kinase 1
4IM2 2.5 Å, Structure of Tank-Binding Kinase 1
5EOA 2.5 Å, Crystal structure of OPTN E50K mutant and TBK1 complex
4EUT 2.6 Å, Structure of BX-795 Complexed with Unphosphorylated Human TBK1 Kinase-ULD Domain
4IWO 2.61 Å, Crystal structure and mechanism of activation of TBK1
6RSU 2.75 Å, TBK1 in complex with Inhibitor compound 35
4IWQ 3.0 Å, Crystal structure and mechanism of activation of TBK1
4IWP 3.06 Å, Crystal structure and mechanism of activation of TBK1

Browse structure collections

About this viewer

MolViewer shows 6RST directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.