2XRW: Mitogen-activated protein kinase 8

Linear binding motifs for JNK and for calcineurin antagonistically control the nuclear shuttling of NFAT4. Determined by X-ray diffraction at 1.33 Å resolution. Released 28 Sept 2011.

Method: X-ray diffraction
Resolution: 1.33 Å
Organism: HOMO SAPIENS
Chains: 2
Atoms: 3,418
Mol. weight: 45.21 kDa
Ligands: ANP
Released: 28 Sept 2011

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

Secondary structure: helices and β-sheets

2XRW contains 25 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: 24 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	4-9	6
β-strand	10-15	6	1
β-strand	18-23	6	1
β-strand	26-34	9	2
β-strand	38-45	8	2
β-strand	50-58	9	2
α-helix	64-79	16
β-strand	85	1	3
α-helix	86-87	2
β-strand	88-92	5	2
β-strand	103-109	7	2
α-helix	110-111	2
β-strand	113-114	2	3
α-helix	115-120	6
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	254-261	8
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	312-317	6
α-helix	319-322	4
α-helix	327-330	4
α-helix	332-335	4
α-helix	337-338	2
α-helix	349-363	15

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	146-148	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mitogen-activated protein kinase 8	A	protein	371	HOMO SAPIENS	P45983 (AlphaFold model)
Nuclear factor of activated T-cells\, cytoplasmic 3	B	protein	14	HOMO SAPIENS	Q12968 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2XRW_1 MITOGEN-ACTIVATED PROTEIN KINASE 8 (chains A)
MGSRSKRDNNFYSVEIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSR
PFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLEEFQDVYIVMELMDANLCQVI
QMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTS
FMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVIE
QLGTPCPEFMKKLQPTVRTYVENRPKYAGYSFEKLFPDVLFPADSEHNKLKASQARDLLS
KMLVIDASKRISVDEALQHPYINVWYDPSEAEAPPPKIPDKQLDEREHTIEEWKELIYKE
VMDLEHHHHHH

Sequence of entity 2 (B), FASTA

>2XRW_2 NUCLEAR FACTOR OF ACTIVATED T-CELLS\, CYTOPLASMIC 3 (chains B)
LERPSRDHLYLPLE

Ligands and cofactors

ID	Name	Formula	Copies
ANP	Phosphoaminophosphonic acid-adenylate ester	C10 H17 N6 O12 P3	1

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

Primary citation

Specificity of Linear Motifs that Bind to a Common Mitogen-Activated Protein Kinase Docking Groove. Garai, A., Zeke, A., Gogl, G. et al. Sci Signal (2012) 5:74. DOI 10.1126/SCISIGNAL.2003004 · PubMed

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

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.
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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