5WJJ: Mitogen-activated protein kinase 14

Structure-based Design, Synthesis, and Biological Evaluation of Imidazo[1,2-b]pyridazine-based p38 MAP Kinase Inhibitors. Determined by X-ray diffraction at 1.6 Å resolution. Released 17 Jan 2018.

Method: X-ray diffraction
Resolution: 1.6 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,160
Mol. weight: 42.17 kDa
Ligands: AQY
Released: 17 Jan 2018

Explore 5WJJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5WJJ contains 25 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: 25 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
β-strand	8-13	6	1
β-strand	16-21	6	1
β-strand	24-33	10	2
β-strand	36-43	8	2
β-strand	48-54	7	2
α-helix	55	1
α-helix	62-77	16
β-strand	83	1	3
β-strand	88-90	3	2
α-helix	96-98	3
β-strand	103-107	5	2
β-strand	112	1	3
α-helix	113-117	5
α-helix	121-123	3
α-helix	124-143	20
α-helix	153-155	3
β-strand	156-158	3	3
β-strand	164-166	3	3
α-helix	170-174	5
α-helix	185-188	4
α-helix	191-194	4
α-helix	204-218	15
α-helix	228-239	12
α-helix	244-247	4
α-helix	253-259	7
α-helix	265-268	4
α-helix	270-272	3
α-helix	279-288	10
α-helix	293-295	3
α-helix	297-298	2
α-helix	299-303	5
α-helix	306-308	3
α-helix	320-322	3
α-helix	326-329	4
α-helix	334-347	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mitogen-activated protein kinase 14	A	protein	365	Homo sapiens	Q16539 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5WJJ_1 Mitogen-activated protein kinase 14 (chains A)
GAMGSMSQERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKL
SRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNN
IVKSQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDSELKILDFGLARHT
DDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLI
LRLVGTPGAELLKKISSESARNYIQSLTQMPKMNFANVFIGANPLAVDLLEKMLVLDSDK
RITAAQALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTYDEVISFVPPPLDQ
EEMES

Ligands and cofactors

ID	Name	Formula	Copies
AQY	N-{4-[2-(4-fluoro-3-methylphenyl)imidazo[1,2-b]pyridazin-3-yl]pyridin-2-yl}-2-m…	C25 H19 F N6 O2	1

Primary citation

Structure-based design, synthesis, and biological evaluation of imidazo[1,2-b]pyridazine-based p38 MAP kinase inhibitors. Kaieda, A., Takahashi, M., Takai, T. et al. Bioorg Med Chem (2018) 26:647-660. DOI 10.1016/j.bmc.2017.12.031 · PubMed

Other PDB entries of the same protein (UniProt Q16539 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2FST 1.45 Å, mitogen activated protein kinase p38alpha (D176A+F327L) activating mutant
3LFF 1.5 Å, Human p38 MAP Kinase in Complex with RL166
3OEF 1.6 Å, Crystal structure of Y323F inactive mutant of p38alpha MAP kinase
3ZS5 1.6 Å, Structural basis for kinase selectivity of three clinical p38alpha inhibitors
4EHV 1.6 Å, Human p38 MAP kinase in complex with NP-F10 and RL87
6SFI 1.6 Å, Crystal structure of p38 alpha in complex with compound 75 (MCP33)
9MHB 1.65 Å, Crystal Structure of Human P38 alpha MAPK In Complex with MW01-14-064SRM
4GEO 1.66 Å, P38a MAP kinase DEF-pocket penta mutant (M194A, L195A, H228A, I229A, Y258A)
6QYX 1.66 Å, p38(alpha) MAP kinase with the activation loop of ERK2
8YD9 1.66 Å, Crystal structure of p38alpha with an allosteric inhibitor 3
2FSL 1.7 Å, mitogen activated protein kinase p38alpha (D176A+F327S) activating mutant form-A
2QD9 1.7 Å, P38 Alpha Map Kinase inhibitor based on heterobicyclic scaffolds

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