4L53: PDB entry 4L53

Crystal Structure of (1R,4R)-4-{4-[7-amino-2-(1,2,3-benzothiadiazol-7-yl)-3-chlorofuro[2,3-c]pyridin-4-yl]-1H-pyrazol-1-yl}cyclohexan-1-ol bound to TAK1-TAB1. Determined by X-ray diffraction at 2.55 Å resolution. Released 3 Jul 2013.

Method: X-ray diffraction
Resolution: 2.55 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,440
Mol. weight: 35.3 kDa
Ligands: 1UO
Released: 3 Jul 2013

Explore 4L53 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4L53 contains 19 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: 19 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	30	1	1
α-helix	33-35	3
β-strand	37-43	7	1
β-strand	49-54	6	1
β-strand	59-64	6	1
α-helix	68-70	3
α-helix	71-81	11
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	159-161	3
β-strand	162-165	4	2
α-helix	166-168	3
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
β-strand	301-302	2	3
β-strand	478	1	4
α-helix	485-494	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mitogen-activated protein kinase kinase kinase 7, TGF-beta-activated kinase 1 and MAP3K7-binding…	A	protein	307	Homo sapiens	O43318 (AlphaFold model), Q15750 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4L53_1 Mitogen-activated protein kinase kinase kinase 7, TGF-beta-activated kinase 1 and MAP3K7-binding protein 1 chimera (chains A)
GSLHMIDYKEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIVELRQLSRVN
HPNIVKLYGACLNPVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLH
SMQPKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNNKGSAAWMAPEVFEGSN
YSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTR
CWSKDPSQRPSMEEIVKIMTHLMRYFPGADEPLQYPCQHSLPPGEDGRVEPYVDFAEFYR
LWSVDHG

Ligands and cofactors

ID	Name	Formula	Copies
1UO	trans-4-{4-[7-amino-2-(1,2,3-benzothiadiazol-7-yl)-3-chlorofuro[2,3-c]pyridin-4…	C22 H19 Cl N6 O2 S	1

Water and common crystallization additives (EDO) are not listed.

Primary citation

Discovery of 7-aminofuro[2,3-c]pyridine inhibitors of TAK1: Optimization of kinase selectivity and pharmacokinetics. Hornberger, K.R., Chen, X., Crew, A.P. et al. Bioorg Med Chem Lett (2013) 23:4511-4516. DOI 10.1016/j.bmcl.2013.06.054 · 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
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

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