4QTD: Human JNK1

Structure of human JNK1 in complex with SCH772984 and the AMPPNP-hydrolysed triphosphate revealing the second type-I binding mode. Determined by X-ray diffraction at 1.5 Å resolution. Released 23 Jul 2014.

Method: X-ray diffraction
Resolution: 1.5 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,521
Mol. weight: 44.78 kDa
Ligands: MG, ANP, 38Z
Released: 23 Jul 2014

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

Secondary structure: helices and β-sheets

4QTD contains 22 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: 22 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	50-58	9	2
α-helix	60-62	3
α-helix	64-79	16
β-strand	85	1	3
β-strand	88-92	5	2
β-strand	103-109	7	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	246-249	4
α-helix	254-262	9
α-helix	264-265	2
α-helix	271-274	4
α-helix	277-279	3
α-helix	285-301	17
α-helix	306-308	3
α-helix	310-311	2
α-helix	312-316	5
α-helix	322-324	3
α-helix	327-330	4
α-helix	332-335	4
α-helix	349-361	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mitogen-activated protein kinase 8	A	protein	364	Homo sapiens	P45983 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4QTD_1 Mitogen-activated protein kinase 8 (chains A)
SMSRSKRDNNFYSVEIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSR
PFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLEEFQDVYIVMELMDANLCQVI
QMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTS
FMMTPYVVTRYYRAPEVILGMGYKENVDLWSVGCIMGEMVCHKILFPGRDYIDQWNKVIE
QLGTPCPEFMKKLQPTVRTYVENRPKYAGYSFEKLFPDVLFPADSEHNKLKASQARDLLS
KMLVIDASKRISVDEALQHPYINVWYDPSEAEAPPPKIPDKQLDEREHTIEEWKELIYKE
VMDL

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	1
ANP	Phosphoaminophosphonic acid-adenylate ester	C10 H17 N6 O12 P3	1
38Z	(3R)-1-(2-oxo-2-{4-[4-(pyrimidin-2-yl)phenyl]piperazin-1-yl}ethyl)-N-[3-(pyridi…	C33 H33 N9 O2	1

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

Primary citation

A unique inhibitor binding site in ERK1/2 is associated with slow binding kinetics. Chaikuad, A., M C Tacconi, E., Zimmer, J. et al. Nat Chem Biol (2014) 10:853-860. DOI 10.1038/nchembio.1629 · 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
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.
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…

Browse structure collections

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