2QD9: Mitogen-activated protein kinase 14

P38 Alpha Map Kinase inhibitor based on heterobicyclic scaffolds. Determined by X-ray diffraction at 1.7 Å resolution. Released 21 Aug 2007.

Method: X-ray diffraction
Resolution: 1.7 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,850
Mol. weight: 42.66 kDa
Ligands: LGF
Released: 21 Aug 2007

Explore 2QD9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2QD9 contains 20 α-helices and 12 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: 20 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	8-13	6	1
β-strand	16-21	6	1
β-strand	24-29	6	2
β-strand	36-43	8	2
β-strand	49-55	7	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	113-116	4
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	204-218	15
α-helix	228-239	12
α-helix	244-247	4
α-helix	253-260	8
α-helix	263-264	2
α-helix	266-268	3
α-helix	270-273	4
α-helix	279-288	10
α-helix	293-295	3
α-helix	299-303	5
α-helix	306-308	3
α-helix	314-316	3
α-helix	318-322	5
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	366	Homo sapiens	Q16539 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2QD9_1 Mitogen-activated protein kinase 14 (chains A)
MAHHHHHSQERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKK
LSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLMGADLN
NIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARH
TDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKL
ILRLVGTPGAELLKKISSESARNYIQSLTQMPKMNFANVFIGANPLAVDLLEKMLVLDSD
KRITAAQALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTYDEVISFVPPPLD
QEEMES

Ligands and cofactors

ID	Name	Formula	Copies
LGF	1-[5-[[3-[2,4-bis(fluoranyl)phenyl]-6,8-dihydro-5~{H}-imidazo[1,5-a]pyrazin-7-y…	C27 H24 F2 N6 O5	1

Primary citation

Synthesis and SAR of p38alpha MAP kinase inhibitors based on heterobicyclic scaffolds. Murali Dhar, T.G., Wrobleski, S.T., Lin, S. et al. Bioorg Med Chem Lett (2007) 17:5019-5024. DOI 10.1016/j.bmcl.2007.07.029 · 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
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

Browse structure collections

About this viewer

MolViewer shows 2QD9 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.