4IWP: Serine/threonine-protein kinase TBK1

Crystal structure and mechanism of activation of TBK1. Determined by X-ray diffraction at 3.06 Å resolution. Released 13 Mar 2013.

Method: X-ray diffraction
Resolution: 3.06 Å
Organism: Homo sapiens
Chains: 1
Atoms: 5,096
Mol. weight: 76.46 kDa
Ligands: BX7
Released: 13 Mar 2013

Explore 4IWP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4IWP contains 24 α-helices and 18 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: 24 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	3	1	1
β-strand	7-17	11	1
β-strand	21-28	8	1
β-strand	34-40	7	1
α-helix	51-61	11
β-strand	67	1	2
α-helix	68-69	2
β-strand	70-75	6	1
β-strand	82-87	6	1
α-helix	88	1
β-strand	93	1	2
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	2
β-strand	151-155	5	2
α-helix	182-185	4
α-helix	201-216	16
β-strand	221-222	2	3
α-helix	232-240	9
β-strand	247-249	3	3
β-strand	258-260	3	3
α-helix	271-284	14
α-helix	295-307	13
β-strand	309-315	7	4
β-strand	320-326	7	4
α-helix	332-343	12
α-helix	347-349	3
β-strand	351-354	4	4
β-strand	357-358	2	4
α-helix	367-369	3
α-helix	370-372	3
β-strand	379-382	4	4
α-helix	398-403	6
α-helix	408-478	71
α-helix	493-526	34
α-helix	534-536	3
α-helix	548-572	25
α-helix	577-600	24
α-helix	601-606	6
α-helix	607-639	33

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein kinase TBK1	A	protein	659	Homo sapiens	Q9UHD2 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4IWP_1 Serine/threonine-protein kinase TBK1 (chains A)
AMGQSTSNHLWLLSDILGQGATANVFRGRHKKTGDLFAIKVFNNISFLRPVDVQMREFEV
LKKLNHKNIVKLFAIEEETTTRHKVLIMEFCPCGSLYTVLEEPSNAYGLPESEFLIVLRD
VVGGMNHLRENGIVHRDIKPGNIMRVIGEDGQSVYKLTDFGAARELEDDEQFVALYGTEE
YLHPDMYERAVLRKDHQKKYGATVDLWSIGVTFYHAATGSLPFRPFEGPRRNKEVMYKII
TGKPSGAISGVQKAENGPIDWSGDMPVSCSLSRGLQVLLTPVLANILEADQEKCWGFDQF
FAETSDILHRMVIHVFSLQQMTAHKIYIHSYNTATIFHELVYKQTKIISSNQELIYEGRR
LVLEPGRLAQHFPKTTEENPIFVVSREPLNTIGLIYEKISLPKVHPRYDLDGDASMAKAI
TGVVCYACRIASTLLLYQELMRKGIRWLIELIKDDYNETVHKKTEVVITLDFCIRNIEKT
VKVYEKLMKINLEAAELGEISDIHTKLLRLSSSQGTIETSLQDIDSRLSPGGSLADAWAH
QEGTHPKDRNVEKLQVLLNCMTEIYYQFKKDKAERRLAYNEEQIHKFDKQKLYYHATKAM
THFTDECVKKYEAFLNKSEEWIRKMLHLRKQLLSLTNQCFDIEEEVSKYQEYTNELQET

Ligands and cofactors

ID	Name	Formula	Copies
BX7	N-(3-{[5-iodo-4-({3-[(thiophen-2-ylcarbonyl)amino]propyl}amino)pyrimidin-2-yl]a…	C23 H26 I N7 O2 S	1

Primary citation

Crystal structure and mechanism of activation of TANK-binding kinase 1. Larabi, A., Devos, J.M., Ng, S.L. et al. Cell Rep (2013) 3:734-746. DOI 10.1016/j.celrep.2013.01.034 · 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
6RSR 3.15 Å, TBK1 in complex with compound 2

Browse structure collections

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