4L7F: Co-crystal Structure of JNK1 and AX13587

Co-crystal Structure of JNK1 and AX13587. Determined by X-ray diffraction at 1.95 Å resolution. Released 21 Aug 2013.

Method: X-ray diffraction
Resolution: 1.95 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,554
Mol. weight: 42.84 kDa
Ligands: 1V5
Released: 21 Aug 2013

Explore 4L7F in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4L7F contains 21 α-helices and 11 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: 21 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	10-15	6	1
β-strand	18-23	6	1
β-strand	26-33	8	2
β-strand	39-45	7	2
β-strand	50-58	9	2
α-helix	64-79	16
β-strand	85	1	3
β-strand	90-92	3	2
β-strand	103-109	7	2
β-strand	113-114	2	3
α-helix	115-119	5
α-helix	125-143	19
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	246-249	4
α-helix	254-262	9
α-helix	264-265	2
α-helix	271-274	4
α-helix	277-279	3
α-helix	281	1
α-helix	291-301	11
α-helix	310-311	2
α-helix	312-317	6
α-helix	322-324	3
α-helix	327-330	4
α-helix	332-335	4
α-helix	349-365	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mitogen-activated protein kinase 8	A	protein	367	Homo sapiens	P45983 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4L7F_1 Mitogen-activated protein kinase 8 (chains A)
SLDNNFYSVEIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQ
THAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLEEFQDVYIVMELMDANLCQVIQMELD
HERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTP
YVVTRYYRAPEVILGMGYKENVDLWSVGCIMGEMVCHKILFPGRDYIDQWNKVIEQLGTP
CPEFMKKLQPTVRTYVENRPKYAGYSFEKLFPDVLFPADSEHNKLKASQARDLLSKMLVI
DASKRISVDEALQHPYINVWYDPSEAEAPPPKIPDKQLDEREHTIEEWKELIYKEVMDWR
KGIITIT

Ligands and cofactors

ID	Name	Formula	Copies
1V5	N-[1-(4-fluorophenyl)cyclopropyl]-4-[(trans-4-hydroxycyclohexyl)amino]imidazo[1…	C26 H26 F N5 O2	1

Primary citation

Hit-to-lead optimization and kinase selectivity of imidazo[1,2-a]quinoxalin-4-amine derived JNK1 inhibitors. Li, B., Cociorva, O.M., Nomanbhoy, T. et al. Bioorg Med Chem Lett (2013) 23:5217-5222. DOI 10.1016/j.bmcl.2013.06.087 · 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.
3PZE 2.0 Å, JNK1 in complex with inhibitor
8X5M 2.0 Å, The Crystal Structure of JNK1 from Biortus.
4HYU 2.15 Å, Crystal structure of JNK1 in complex with JIP1 peptide and…
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…

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