Target Binding Site Detail

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Target General Information
Ligand General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T55398 Target Info
Target Name Renal carcinoma antigen NY-REN-64 (IRAK-4)
Synonyms Interleukin-1 receptor-associated kinase 4; IRAK-4
Target Type Clinical trial Target
Gene Name IRAK4
Biochemical Class Kinase
UniProt ID
IRAK4_HUMAN
Ligand General Information  Top
Ligand Name AMP-PNP Ligand Info
Canonical SMILES C1=NC(=C2C(=N1)N(C=N2)C3C(C(C(O3)COP(=O)(O)OP(=O)(NP(=O)(O)O)O)O)O)N
InChI 1S/C10H17N6O12P3/c11-8-5-9(13-2-12-8)16(3-14-5)10-7(18)6(17)4(27-10)1-26-31(24,25)28-30(22,23)15-29(19,20)21/h2-4,6-7,10,17-18H,1H2,(H,24,25)(H2,11,12,13)(H4,15,19,20,21,22,23)/t4-,6-,7-,10-/m1/s1
InChIKey PVKSNHVPLWYQGJ-KQYNXXCUSA-N
PubChem Compound ID 33113
Drug Binding Sites of Target  Top
PDB ID: 6EGF      Crystal structure of the inactive unphosphorylated IRAK4 kinase domain bound to AMP-PNP
Method X-ray diffraction Resolution 2.61 Å Mutation No [1]
PDB Sequence
RFHSFSFYEL
173
KNVTNNFDER
183
PISVGGNKMG
193
EGGFGVVYKG
203
YVNNTTVAVK
213

KLAAMVDITT
223
EELKQQFDQE
233
IKVMAKCQHE
243
NLVELLGFSS
253
DGDDLCLVYV
263

YMPNGSLLDR
273
LSCLDGTPPL
283
SWHMRCKIAQ
293
GAANGINFLH
303
ENHHIHRNIK
313

SANILLDEAF
323
TAKISDFGLA
333
RASEKTTAYM
355
APEALRGEIT
365
PKSDIYSFGV
375

VLLEIITGLP
385
AVDEHREPQL
395
LLDIKEEIED
405
EEKTIEDYID
415
KKMNDADSTS
425

VEAMYSVASQ
435
CLHEKKNKRP
445
DIKKVQQLLQ
455
EMTAS
Residue
Distance (Å)
MET192
3.279
GLY193
3.865
GLU194
3.634
GLY195
2.995
GLY196
2.636
PHE197
4.504
GLY198
4.080
VAL200
3.265
ALA211
3.613
LYS213
2.695
VAL246
4.177
TYR262
3.948
VAL263
2.908
Residue
Distance (Å)
TYR264
3.703
MET265
2.946
GLY268
4.664
SER269
3.297
ASP272
4.130
ASN311
2.740
LYS313
2.908
ALA315
2.972
ASN316
2.698
LEU318
3.381
SER328
4.944
ASP329
2.646
PDB ID: 2OID      Crystal structure of IRAK4 kinase domain complexed with AMPPNP
Method X-ray diffraction Resolution 2.30 Å Mutation Yes [2]
PDB Sequence
RFHSFSFYEL
173
KNVTNNFDER
183
PISVGGNKGE
194
GGFGVVYKGY
204
VNNTTVAVKK
214

EIKVMAKCQH
242
ENLVELLGFS
252
CLVYVYMPNG
268
SLLDRLSCLD
278
GTPPLSWHMR
288

CKIAQGAANG
298
INFLHENHHI
308
HRDIKSANIL
318
LDEAFTAKIS
328
DFGLARASEV
343

MRIVGTTAYM
355
APEALRGEIT
365
PKSDIYSFGV
375
VLLEIITGLP
385
AVDEHREPQL
395

LLDIKEEIED
405
EEKTIEDYID
415
KKMNDADSTS
425
VEAMYSVASQ
435
CLHEKKNKRP
445

DIKKVQQLLQ
455
EMT
Residue
Distance (Å)
GLY193
3.395
GLU194
3.358
GLY195
3.310
GLY196
3.009
PHE197
4.355
GLY198
4.125
VAL200
3.128
ALA211
3.738
LYS213
4.117
VAL246
3.843
TYR262
3.417
VAL263
2.980
Residue
Distance (Å)
TYR264
3.824
MET265
3.014
GLY268
4.895
SER269
4.357
ASP272
4.943
ASP311
3.712
LYS313
3.093
ALA315
4.067
ASN316
2.752
LEU318
3.163
ASP329
2.543
THR351
4.693
References  Top
REF 1 Conformational flexibility and inhibitor binding to unphosphorylated interleukin-1 receptor-associated kinase 4 (IRAK4). J Biol Chem. 2019 Mar 22;294(12):4511-4519.
REF 2 Cutting Edge: IL-1 receptor-associated kinase 4 structures reveal novel features and multiple conformations. J Immunol. 2007 Mar 1;178(5):2641-5.

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