2EVA: TAK1 kinase - TAB1 chimera fusion protein

Structural Basis for the Interaction of TAK1 Kinase with its Activating Protein TAB1. Determined by X-ray diffraction at 2.0 Å resolution. Released 2 May 2006.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,597
Mol. weight: 35.05 kDa
Ligands: ADN
Released: 2 May 2006

Explore 2EVA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2EVA contains 19 α-helices and 15 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: 19 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	30	1	1
α-helix	33-35	3
β-strand	36-43	8	2
β-strand	49-55	7	2
β-strand	58-64	7	2
α-helix	70-83	14
β-strand	89	1	3
α-helix	90-91	2
β-strand	92-94	3	2
β-strand	95	1	1
β-strand	101-105	5	2
β-strand	111	1	3
α-helix	112-117	6
β-strand	122-123	2	4
α-helix	124	1
α-helix	127-145	19
α-helix	151-153	3
α-helix	159-161	3
β-strand	162-165	4	3
β-strand	170-173	4	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	5
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	297-298	2
β-strand	301-302	2	4
β-strand	478	1	5
α-helix	485-494	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
TAK1 kinase - TAB1 chimera fusion protein	A	protein	307	Homo sapiens	O43318 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2EVA_1 TAK1 kinase - TAB1 chimera fusion protein (chains A)
SLHMIDYKEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIVELRQLSRVNH
PNIVKLYGACLNPVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHS
MQPKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNNKGSAAWMAPEVFEGSNY
SEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTRC
WSKDPSQRPSMEEIVKIMTHLMRYFPGADEPLQYPCQHSLPPGEDGRVEPYVDFAEFYRL
WSVDHGE

Ligands and cofactors

ID	Name	Formula	Copies
ADN	Adenosine	C10 H13 N5 O4	1

Primary citation

Structural basis for the interaction of TAK1 kinase with its activating protein TAB1. Brown, K., Vial, S.C., Dedi, N. et al. J Mol Biol (2005) 354:1013-1020. DOI 10.1016/j.jmb.2005.09.098 · 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
5JGA 2.0 Å, Crystal structure of human TAK1/TAB1 fusion protein in complex with ligand 11c
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

Browse structure collections

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