3LFF: Human p38 MAP Kinase

Human p38 MAP Kinase in Complex with RL166. Determined by X-ray diffraction at 1.5 Å resolution. Released 20 Apr 2011.

Method: X-ray diffraction
Resolution: 1.5 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,056
Mol. weight: 42.22 kDa
Ligands: Z83, BOG
Released: 20 Apr 2011

Explore 3LFF in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3LFF 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
α-helix	6-7	2
β-strand	8-13	6	1
β-strand	16-21	6	1
β-strand	24-32	9	2
β-strand	36-43	8	2
β-strand	48-55	8	2
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	111-112	2	3
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	191-194	4
α-helix	203-218	16
α-helix	228-239	12
α-helix	244-247	4
α-helix	253-259	7
α-helix	266-268	3
α-helix	270-273	4
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	334-346	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mitogen-activated protein kinase 14	A	protein	360	Homo sapiens	Q16539 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3LFF_1 Mitogen-activated protein kinase 14 (chains A)
GSQERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQ
SIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKSQ
KLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDSELKILDFGLCRHTDDEMT
GYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVG
TPGAELLKKISSESARNYIQSLTQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAA
QALAHAYFAQYHDPDDEPVADPYDQSLESRDLLIDEWKSLTYDEVISFVPPPLDQEEMES

Ligands and cofactors

ID	Name	Formula	Copies
Z83	(4-{3-tert-butyl-5-[(1,3-thiazol-2-ylcarbamoyl)amino]-1H-pyrazol-1-yl}phenyl)ac…	C19 H21 N5 O3 S	1
BOG	octyl beta-D-glucopyranoside	C14 H28 O6	2

Primary citation

Development of novel thiazole-urea compounds which stabalize the inactive conformation of p38 alpha. Getlik, M., Gruetter, C., Simard, J.R. et al. To be published.

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
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
5WJJ 1.6 Å, Structure-based Design, Synthesis, and Biological Evaluation of…
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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