Crystal structure of the unphosphorylated IRAK4 kinase domain Bound to a type I inhibitor. Determined by X-ray diffraction at 1.4 Å resolution. Released 13 Feb 2019.
Explore 6EGE in 3D Show helices and sheets RCSB PDB PDBe
6EGE contains 36 α-helices and 34 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 166-167 | 2 | 7 |
| α-helix | 170-176 | 7 | |
| β-strand | 184 | 1 | 7 |
| α-helix | 185-187 | 3 | |
| β-strand | 191-195 | 5 | 7 |
| β-strand | 198-205 | 8 | 7 |
| β-strand | 208-215 | 8 | 7 |
| α-helix | 227-239 | 13 | |
| β-strand | 245 | 1 | 8 |
| α-helix | 246-247 | 2 | |
| β-strand | 248-251 | 4 | 7 |
| β-strand | 259-263 | 5 | 7 |
| β-strand | 269 | 1 | 8 |
| α-helix | 270-274 | 5 | |
| α-helix | 277-279 | 3 | |
| α-helix | 280-284 | 5 | |
| α-helix | 285-304 | 20 | |
| β-strand | 308 | 1 | 9 |
| α-helix | 314-316 | 3 | |
| β-strand | 317-319 | 3 | 8 |
| β-strand | 325-327 | 3 | 8 |
| β-strand | 334 | 1 | 9 |
| β-strand | 350-351 | 2 | 5 |
| α-helix | 352-354 | 3 | |
| α-helix | 357-360 | 4 | |
| α-helix | 366-382 | 17 | |
| β-strand | 387 | 1 | 10 |
| β-strand | 395 | 1 | 10 |
| α-helix | 396-398 | 3 | |
| α-helix | 399-404 | 6 | |
| α-helix | 410-413 | 4 | |
| α-helix | 423-436 | 14 | |
| α-helix | 441-443 | 3 | |
| α-helix | 445-446 | 2 | |
| α-helix | 447-458 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 166-167 | 2 | 1 |
| α-helix | 170-176 | 7 | |
| β-strand | 184 | 1 | 1 |
| α-helix | 185-187 | 3 | |
| β-strand | 191-194 | 4 | 1 |
| β-strand | 198-205 | 8 | 1 |
| β-strand | 208-215 | 8 | 1 |
| α-helix | 225-239 | 15 | |
| β-strand | 245 | 1 | 2 |
| β-strand | 248-252 | 5 | 1 |
| β-strand | 259-263 | 5 | 1 |
| β-strand | 269 | 1 | 2 |
| α-helix | 270-274 | 5 | |
| α-helix | 277-279 | 3 | |
| α-helix | 280-284 | 5 | |
| α-helix | 285-304 | 20 | |
| β-strand | 308 | 1 | 3 |
| α-helix | 314-316 | 3 | |
| β-strand | 317-319 | 3 | 2 |
| β-strand | 325-327 | 3 | 2 |
| β-strand | 334 | 1 | 3 |
| β-strand | 338 | 1 | 4 |
| β-strand | 344-345 | 2 | 5 |
| α-helix | 357-360 | 4 | |
| β-strand | 364 | 1 | 4 |
| α-helix | 367-382 | 16 | |
| β-strand | 387 | 1 | 6 |
| β-strand | 395 | 1 | 6 |
| α-helix | 396-398 | 3 | |
| α-helix | 399-405 | 7 | |
| α-helix | 410-413 | 4 | |
| α-helix | 423-436 | 14 | |
| α-helix | 441-443 | 3 | |
| α-helix | 445-446 | 2 | |
| α-helix | 447-456 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Interleukin-1 receptor-associated kinase 4 | A, D | protein | 302 | Homo sapiens | Q9NWZ3 (AlphaFold model) |
>6EGE_1 Interleukin-1 receptor-associated kinase 4 (chains A, D) GAMGSRFHSFSFYELKNVTNNFDERPISVGGNKMGEGGFGVVYKGYVNNTTVAVKKLAAM VDITTEELKQQFDQEIKVMAKCQHENLVELLGFSSDGDDLCLVYVYMPNGSLLDRLSCLD GTPPLSWHMRCKIAQGAANGINFLHENHHIHRNIKSANILLDEAFTAKISDFGLARASEK FAQTVMTSRIVGTTAYMAPEALRGEITPKSDIYSFGVVLLEIITGLPAVDEHREPQLLLD IKEEIEDEEKTIEDYIDKKMNDADSTSVEAMYSVASQCLHEKKNKRPDIKKVQQLLQEMT AS
| ID | Name | Formula | Copies |
|---|---|---|---|
| DL1 | N-[2-methoxy-4-(morpholin-4-yl)phenyl]-6-(1H-pyrazol-5-yl)pyridine-2-carboxamide | C20 H21 N5 O3 | 2 |
Conformational flexibility and inhibitor binding to unphosphorylated interleukin-1 receptor-associated kinase 4 (IRAK4). Wang, L., Ferrao, R., Li, Q. et al. J Biol Chem (2019) 294:4511-4519. DOI 10.1074/jbc.RA118.005428 · PubMed
Other PDB entries of the same protein (UniProt Q9NWZ3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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