5JGA: Human TAK1/TAB1 fusion protein

Crystal structure of human TAK1/TAB1 fusion protein in complex with ligand 11c. Determined by X-ray diffraction at 2.0 Å resolution. Released 27 Jul 2016.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,534
Mol. weight: 36 kDa
Ligands: 6KC
Released: 27 Jul 2016

Explore 5JGA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5JGA contains 20 α-helices and 14 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: 20 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	29-30	2	1
α-helix	33-35	3
β-strand	37-44	8	1
β-strand	49-55	7	1
β-strand	58-64	7	1
α-helix	71-83	13
β-strand	89	1	2
β-strand	92-97	6	1
β-strand	100-105	6	1
β-strand	111	1	2
α-helix	112-117	6
β-strand	122-123	2	3
α-helix	124	1
α-helix	127-145	19
α-helix	151-153	3
α-helix	159-161	3
β-strand	162-165	4	2
β-strand	170-173	4	2
α-helix	193-195	3
α-helix	198-201	4
α-helix	209-224	16
α-helix	236-244	9
α-helix	249-251	3
β-strand	252	1	4
α-helix	257-266	10
α-helix	271-273	3
α-helix	275-276	2
α-helix	277-287	11
α-helix	288-290	3
α-helix	297	1
β-strand	301-302	2	3
α-helix	470-473	4
β-strand	478	1	4
α-helix	485-495	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
TAK1 kinase - TAB1 chimera fusion protein	A	protein	315	Homo sapiens	O43318 (AlphaFold model), Q15750 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5JGA_1 TAK1 kinase - TAB1 chimera fusion protein (chains A)
GPLHMIDYKEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIVELRQLSRVN
HPNIVKLYGACLNPVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLH
SMQPKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNNKGSAAWMAPEVFEGSN
YSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTR
CWSKDPSQRPSMEEIVKIMTHLMRYFPGADEPLQYPCQHSLPPGEDGRVEPYVDFAEFYR
LWSVDHGEQSVVTAP

Ligands and cofactors

ID	Name	Formula	Copies
6KC	N-[5-(4-methylpiperazine-1-carbonyl)[1,1'-biphenyl]-2-yl]-4-oxo-3,4-dihydrothie…	C25 H23 N5 O3 S	1

Primary citation

Discovery of a potent and highly selective transforming growth factor beta receptor-associated kinase 1 (TAK1) inhibitor by structure based drug design (SBDD). Muraoka, T., Ide, M., Morikami, K. et al. Bioorg Med Chem (2016) 24:4206-4217. DOI 10.1016/j.bmc.2016.07.006 · PubMed

Other PDB entries of the same protein (UniProt O43318 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7NTH 1.97 Å, Structure of TAK1 in complex with compound 54
7NTI 1.98 Å, Structure of TAK1 in complex with compound 22
2EVA 2.0 Å, Structural Basis for the Interaction of TAK1 Kinase with its Activating Protein TAB1
5V5N 2.01 Å, Crystal structure of Takinib bound to TAK1
8GW3 2.05 Å, Crystal structure of human TAK1 kinase domain fused with TAB1
5E7R 2.11 Å, Crystal structure of TL10-81 bound to TAK1-TAB1
4GS6 2.2 Å, Irreversible Inhibition of TAK1 Kinase by 5Z-7-Oxozeaenol
5JH6 2.37 Å, Crystal structure of TL10-92 bound to TAK1-TAB1
5J7S 2.37 Å, Crystal structure of SM1-71 bound to TAK1-TAB1
5JK3 2.37 Å, Crystal structure of TL11-128 bound to TAK1-TAB1
4O91 2.39 Å, Crystal Structure of type II inhibitor NG25 bound to TAK1-TAB1
9FPD 2.4 Å, Crystal structure of human TAK1/TAB1 fusion protein in complex with compound S1

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