4HYU: JNK1

Crystal structure of JNK1 in complex with JIP1 peptide and 4-{4-[4-(3-Methanesulfonyl-propoxy)-indazol-1-yl]-pyrimidin-2-ylamino}-cyclohexan. Determined by X-ray diffraction at 2.15 Å resolution. Released 30 Oct 2013.

Method: X-ray diffraction
Resolution: 2.15 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,781
Mol. weight: 44.38 kDa
Ligands: 1BK
Released: 30 Oct 2013

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

Secondary structure: helices and β-sheets

4HYU contains 21 α-helices and 11 β-strands across 2 chains. 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, 11 β-strands

Element	Residues	Length	Sheet
β-strand	10-15	6	1
β-strand	18-23	6	1
β-strand	26-35	10	2
β-strand	38-45	8	2
β-strand	50-57	8	2
α-helix	64-79	16
β-strand	85	1	3
β-strand	90-92	3	2
β-strand	105-109	5	2
β-strand	113-114	2	3
α-helix	115-118	4
α-helix	125-144	20
α-helix	154-156	3
β-strand	157-159	3	3
β-strand	165-167	3	3
α-helix	194-197	4
α-helix	206-220	15
α-helix	230-241	12
α-helix	243-245	3
α-helix	246-250	5
α-helix	254-260	7
α-helix	264-265	2
α-helix	271-274	4
α-helix	277-279	3
α-helix	290-301	12
α-helix	306-308	3
α-helix	310-311	2
α-helix	312-317	6
α-helix	319-322	4
α-helix	327-330	4
α-helix	349-360	12

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	155-157	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mitogen-activated protein kinase 8	A	protein	369	Homo sapiens	P45983 (AlphaFold model)
C-Jun-amino-terminal kinase-interacting protein 1	B	protein	11	Homo sapiens	Q9UQF2 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4HYU_1 Mitogen-activated protein kinase 8 (chains A)
MSRSKRDNNFYSVEIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRP
FQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLEEFQDVYIVMELMDANLCQVIQ
MELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSF
MMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVIEQ
LGTPCPEFMKKLQPTVRTYVENRPKYAGYSFEKLFPDVLFPADSEHNKLKASQARDLLSK
MLVIDASKRISVDEALQHPYINVWYDPSEAEAPPPKIPDKQLDEREHTIEEWKELIYKEV
MDLHHHHHH

Sequence of entity 2 (B), FASTA

>4HYU_2 C-Jun-amino-terminal kinase-interacting protein 1 (chains B)
RPKRPTTLNLF

Ligands and cofactors

ID	Name	Formula	Copies
1BK	trans-4-[(4-{4-[3-(methylsulfonyl)propoxy]-1H-indazol-1-yl}pyrimidin-2-yl)amino…	C21 H27 N5 O4 S	1

Primary citation

Development of amino-pyrimidine inhibitors of c-Jun N-terminal kinase (JNK): kinase profiling guided optimization of a 1,2,3-benzotriazole lead. Palmer, W.S., Alam, M., Arzeno, H.B. et al. Bioorg Med Chem Lett (2013) 23:1486-1492. DOI 10.1016/j.bmcl.2012.12.047 · PubMed

Other PDB entries of the same protein (UniProt P45983 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2XRW 1.33 Å, Linear binding motifs for JNK and for calcineurin antagonistically control the nuclear…
12CV 1.5 Å, Crystal Structure of human JNK1 Kinase Domain in complex with inhibitor CCD-2728
4QTD 1.5 Å, Structure of human JNK1 in complex with SCH772984 and the AMPPNP-hydrolysed triphosphate…
11ZL 1.55 Å, Crystal Structure of human JNK1 Kinase Domain in complex with inhibitor CCD-3013
8R5E 1.7 Å, JNK1 covalently bound to RU77 cyclohexenone based inhibitor
3ELJ 1.8 Å, Jnk1 complexed with a bis-anilino-pyrrolopyrimidine inhibitor.
4AWI 1.91 Å, Human Jnk1alpha kinase with 4-phenyl-7-azaindole IKK2 inhibitor.
4L7F 1.95 Å, Co-crystal Structure of JNK1 and AX13587
3PZE 2.0 Å, JNK1 in complex with inhibitor
8X5M 2.0 Å, The Crystal Structure of JNK1 from Biortus.
4E73 2.27 Å, Crystal structure of JNK1beta-JIP in complex with an azaquinolone inhbitor
4IZY 2.3 Å, Crystal structure of JNK1 in complex with JIP1 peptide and…

Browse structure collections

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