1LEW: Mitogen-activated protein kinase 14

Crystal structure of map kinase P38 complexed to the docking site on its nuclear substrate MEF2A. Determined by X-ray diffraction at 2.3 Å resolution. Released 10 Jul 2002.

Method: X-ray diffraction
Resolution: 2.3 Å
Organisms: Mus musculus, Homo sapiens
Chains: 2
Atoms: 2,955
Mol. weight: 42.72 kDa
Released: 10 Jul 2002

Explore 1LEW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1LEW contains 24 α-helices and 12 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: 23 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	8-13	6	1
β-strand	16-21	6	1
β-strand	24-31	8	2
β-strand	36-43	8	2
β-strand	48-55	8	2
α-helix	62-77	16
β-strand	80	1	3
β-strand	83	1	3
β-strand	88-90	3	2
β-strand	103-107	5	2
β-strand	111-112	2	3
α-helix	113-119	7
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	185-188	4
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	266-268	3
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	314-316	3
α-helix	326-329	4
α-helix	334-346	13
α-helix	350-353	4

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	8-10	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mitogen-activated protein kinase 14	A	protein	360	Mus musculus	P47811 (AlphaFold model)
Myocyte-specific enhancer factor 2A	B	protein	12	Homo sapiens	Q02078 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1LEW_1 Mitogen-activated protein kinase 14 (chains A)
MSQERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGHRVAVKKLSRPFQ
SIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKCQ
KLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMT
GYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVG
TPGAELLKKISSESARNYIQSLAQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAA
QALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTYDEVISFVPPPLDQEEMES

Sequence of entity 2 (B), FASTA

>1LEW_2 Myocyte-specific enhancer factor 2A (chains B)
RKPDLRVVIPPS

Primary citation

Crystal structures of MAP kinase p38 complexed to the docking sites on its nuclear substrate MEF2A and activator MKK3b. Chang, C.I., Xu, B.E., Akella, R. et al. Mol Cell (2002) 9:1241-1249. DOI 10.1016/S1097-2765(02)00525-7 · PubMed

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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