5LAR: P38 alpha MAPK14

Crystal structure of p38 alpha MAPK14 in complex with VPC00628. Determined by X-ray diffraction at 1.5 Å resolution. Released 6 Jul 2016.

Method: X-ray diffraction
Resolution: 1.5 Å
Organism: Mus musculus
Chains: 1
Atoms: 3,297
Mol. weight: 41.9 kDa
Ligands: 6SH
Released: 6 Jul 2016

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

Secondary structure: helices and β-sheets

5LAR contains 30 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: 30 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	5-7	3
β-strand	8-13	6	1
β-strand	16-21	6	1
β-strand	24-30	7	2
α-helix	31-33	3
β-strand	37-43	7	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
α-helix	108-109	2
β-strand	111-112	2	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	171-173	3
α-helix	176-180	5
α-helix	191-194	4
α-helix	203-218	16
α-helix	228-239	12
α-helix	242-243	2
α-helix	244-247	4
α-helix	253-261	9
α-helix	263-264	2
α-helix	266-269	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	334-346	13
α-helix	350-352	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mitogen-activated protein kinase 14	A	protein	361	Mus musculus	P47811 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5LAR_1 Mitogen-activated protein kinase 14 (chains A)
GMSQERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGHRVAVKKLSRPF
QSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKC
QKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEM
TGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLV
GTPGAELLKKISSESARNYIQSLAQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITA
AQALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTYDEVISFVPPPLDQEEME
S

Ligands and cofactors

ID	Name	Formula	Copies
6SH	5-azanyl-~{N}-[[4-[[(2~{S})-1-azanyl-4-cyclohexyl-1-oxidanylidene-butan-2-yl]ca…	C28 H34 N6 O3	1

Primary citation

Novel p38alpha MAP kinase inhibitors identified from yoctoReactor DNA-encoded small molecule library. Petersen, L.K., Blakskaer, P., Chaikuad, A. et al. Medchemcomm (2016) 7:1332-1339. DOI 10.1039/C6MD00241B

Other PDB entries of the same protein (UniProt P47811 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6SP9 1.22 Å, Fragment KCL802 in complex with MAP kinase p38-alpha
6Y80 1.24 Å, Fragment KCL_916 in complex with MAP kinase p38-alpha
6SOV 1.31 Å, Fragments KCL_615 and KCL_802 in complex with MAP kinase p38-alpha
6YCW 1.34 Å, Fragment KCL_K767 in complex with MAP kinase p38-alpha
6Y7Z 1.35 Å, Fragment KCL_914 in complex with MAP kinase p38-alpha
6YCU 1.35 Å, Fragment KCL_K777 in complex with MAP kinase p38-alpha
6Y8H 1.37 Å, Novel p38-alpha crystal lattice with highly exposed p38/TAB1 non-canonical PPI surface.
6SPL 1.38 Å, Fragment KCL615 in complex with MAP kinase p38-alpha
6Y7W 1.39 Å, Fragment KCL_1337 in complex with MAP kinase p38-alpha
5R97 1.44 Å, PanDDA analysis group deposition Form1 MAP kinase p38-alpha -- Fragment N13662a in…
6Y82 1.44 Å, Fragment KCL_804 in complex with MAP kinase p38-alpha
5R94 1.45 Å, PanDDA analysis group deposition Form1 MAP kinase p38-alpha -- Fragment KCL081 in…

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