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 T00663 Target Info
Target Name Stress-activated protein kinase JNK3 (JNK3)
Synonyms Stress-activated protein kinase 1b; SAPK1b; PRKM10; Mitogen-activated protein kinase 10; MAPK 10; MAP kinase p49 3F12; MAP kinase 10; JNK3A; C-Jun N-terminal kinase 3
Target Type Patented-recorded Target
Gene Name MAPK10
Biochemical Class Kinase
UniProt ID
MK10_HUMAN
Ligand General Information  Top
Ligand Name Hydroxyethylcysteine Ligand Info
Canonical SMILES C(CSCC(C(=O)O)N)O
InChI 1S/C5H11NO3S/c6-4(5(8)9)3-10-2-1-7/h4,7H,1-3,6H2,(H,8,9)/t4-/m0/s1
InChIKey MWFRVMDVLYIXJF-BYPYZUCNSA-N
PubChem Compound ID 119224
Drug Binding Sites of Target  Top
PDB ID: 3FI3      Crystal structure of JNK3 with indazole inhibitor, SR-3737
Method X-ray diffraction Resolution 2.20 Å Mutation No [1]
PDB Sequence
DNQFYSVEVG
54
DSTFTVLKRY
64
QNLKPIGIVC
79
AAYDAVLDRN
89
VAIKKLSRPF
99

QNQTHAKRAY
109
RELVLMKVNH
120
KNIISLLNVF
130
TPQKTLEEFQ
140
DVYLVMELMD
150

ANLQVIQMEL
161
DHERMSYLLY
171
QMLGIKHLHS
182
AGIIHRDLKP
192
SNIVVKSDTL
203

KILDFGLARV
225
TRYYRAPEVI
235
LGMGYKENVD
245
IWSVGCIMGE
255
MVRHKILFPG
265

RDYIDQWNKV
275
IEQLGTPCPE
285
FMKKLQPTVR
295
NYVENRPKYA
305
GLTFPKLFPD
315

SLFPADSEHN
325
KLKASQARDL
335
LSKMLVIDPA
345
KRISVDDALQ
355
HPYINVWYPP
373

QIYDKQLDER
383
EHTIEEWKEL
393
IYKEVMNS
Residue
Distance (Å)
VAL113
3.288
LEU114
3.182
MET115
3.537
LYS116
1.329
VAL118
1.325
ASN119
3.537
HIS120
2.883
ASN122
3.672
ASN152
3.073
LEU153
1.329
GLN155
1.327
VAL156
3.394
ILE157
3.599
GLN158
3.670
MET159
4.497
ARG165
3.434
TYR168
3.450
LEU169
3.475
LEU170
4.779
TYR171
2.936
GLN172
2.956
MET173
3.271
LEU174
1.335
Residue
Distance (Å)
GLY176
1.326
ILE177
3.312
LYS178
3.452
HIS179
3.089
ALA183
4.766
PRO192
3.449
SER193
3.836
VAL197
4.033
LYS198
2.882
SER199
3.085
ASP200
1.317
THR202
1.353
LEU203
3.582
TYR229
2.844
GLU255
3.521
ILE261
4.390
LEU354
4.291
GLN374
3.301
ILE375
4.155
TYR376
3.928
ASP377
3.828
LEU380
4.251
PDB ID: 3KVX      JNK3 bound to aminopyrimidine inhibitor, SR-3562
Method X-ray diffraction Resolution 2.40 Å Mutation No [2]
PDB Sequence
NQFYSVEVGD
55
STFTVLKRYQ
65
NLKPIGSGAQ
75
GIVCAAYDAV
85
LDRNVAIKKL
95

SRPFQNQTHA
105
KRAYRELVLM
115
KCVNHKNIIS
125
LLNVFTPQKT
135
LEEFQDVYLV
145

MELMDANLQV
156
IQMELDHERM
166
SYLLYQMLGI
177
KHLHSAGIIH
187
RDLKPSNIVV
197

KSDTLKILDF
208
GLARVTRYYR
230
APEVILGMGY
240
KENVDIWSVG
250
CIMGEMVRHK
260

ILFPGRDYID
270
QWNKVIEQLG
280
TPCPEFMKKL
290
QPTVRNYVEN
300
RPKYAGLTFP
310

KLFPDSLFPA
320
DSEHNKLKAS
330
QARDLLSKML
340
VIDPAKRISV
350
DDALQHPYIN
360

VWYDPAEERE
384
HTIEEWKELI
394
YKEVMNS
Residue
Distance (Å)
HIS120
3.399
ASN122
4.154
ASN152
3.003
LEU153
1.352
GLN155
1.319
VAL156
3.371
ILE157
3.481
GLN158
3.388
MET159
4.398
ARG165
4.835
TYR168
3.614
LEU169
3.471
LEU170
4.903
TYR171
2.960
GLN172
2.888
MET173
3.267
LEU174
1.316
Residue
Distance (Å)
GLY176
1.328
ILE177
3.089
LYS178
3.142
HIS179
2.832
LEU180
4.978
PRO192
3.621
SER193
4.294
VAL197
4.537
LYS198
2.908
SER199
3.271
ASP200
1.360
THR202
1.335
LEU203
3.631
TYR229
4.460
GLU255
3.702
LEU354
4.136
PDB ID: 2R9S      c-Jun N-terminal Kinase 3 with 3,5-Disubstituted Quinoline inhibitor
Method X-ray diffraction Resolution 2.40 Å Mutation Yes [3]
PDB Sequence
NQFYSVEVGD
55
STFTVLKRYQ
65
NLKPIGSGAQ
75
GIVCAAYDAV
85
LDRNVAIKKL
95

SRPFQNQTHA
105
KRAYRELVLM
115
KCVNHKNIIS
125
LLNVFTPQKT
135
LEEFQDVYLV
145

MELMDANLQV
156
IQMELDHERM
166
SYLLYQMLGI
177
KHLHSAGIIH
187
RDLKPSNIVV
197

KSDTLKILDF
208
GLARYYRAPE
233
VILGMGYKEN
243
VDIWSVGCIM
253
GEMVRHKILF
263

PGRDYIDQWN
273
KVIEQLGTPC
283
PEFMKKLQPT
293
VRNYVENRPK
303
YAGLTFPKLF
313

PDSLFPADSE
323
HNKLKASQAR
333
DLLSKMLVID
343
PAKRISVDDA
353
LQHPYINVWY
363

DKQLDEREHT
386
IEEWKELIYK
396
EVMNS
Residue
Distance (Å)
HIS120
3.931
LYS121
3.769
ASN122
3.403
ASN152
2.710
LEU153
1.327
GLN155
1.336
VAL156
3.564
ILE157
3.648
GLN158
3.244
MET159
4.671
ARG165
3.569
TYR168
3.522
LEU169
3.596
LEU170
4.975
TYR171
2.868
GLN172
2.869
MET173
3.325
Residue
Distance (Å)
LEU174
1.342
GLY176
1.324
ILE177
3.294
LYS178
3.438
HIS179
2.971
PRO192
3.571
SER193
4.109
VAL197
4.223
LYS198
2.747
SER199
3.147
ASP200
1.331
THR202
1.328
LEU203
3.389
TYR229
3.099
GLU255
3.398
ILE261
4.382
LEU354
3.673
PDB ID: 3FV8      JNK3 bound to piperazine amide inhibitor, SR2774.
Method X-ray diffraction Resolution 2.28 Å Mutation No [4]
PDB Sequence
.
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .OCY or .OCY2 or .OCY3 or :3OCY;style chemicals stick;color identity;select .A:113 or .A:114 or .A:115 or .A:116 or .A:118 or .A:119 or .A:152 or .A:153 or .A:155 or .A:156 or .A:157 or .A:158 or .A:159 or .A:165 or .A:168 or .A:169 or .A:172 or .A:183 or .A:192 or .A:193 or .A:197 or .A:198 or .A:199 or .A:200 or .A:202 or .A:203 or .A:229 or .A:255 or .A:261 or .A:704; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
VAL113
2.942
LEU114
3.411
MET115
3.527
LYS116
1.327
VAL118
1.327
ASN119
3.801
ASN152
3.015
LEU153
1.331
GLN155
1.325
VAL156
3.455
ILE157
4.053
GLN158
3.485
MET159
4.664
ARG165
3.729
TYR168
3.609
Residue
Distance (Å)
LEU169
3.419
GLN172
3.080
ALA183
4.458
PRO192
3.529
SER193
3.936
VAL197
4.386
LYS198
2.961
SER199
3.087
ASP200
1.318
THR202
1.370
LEU203
3.588
TYR229
3.180
GLU255
3.551
ILE261
4.484
UNK704
2.926
PDB ID: 3FI2      Crystal structure of JNK3 with amino-pyrazole inhibitor, SR-3451
Method X-ray diffraction Resolution 2.28 Å Mutation No [1]
PDB Sequence
.
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .OCY or .OCY2 or .OCY3 or :3OCY;style chemicals stick;color identity;select .A:113 or .A:114 or .A:115 or .A:116 or .A:118 or .A:119 or .A:156 or .A:159 or .A:165 or .A:168 or .A:169 or .A:172 or .A:197 or .A:198 or .A:199 or .A:200 or .A:202 or .A:203 or .A:505; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
VAL113
3.136
LEU114
3.223
MET115
3.424
LYS116
1.329
VAL118
1.327
ASN119
3.664
VAL156
3.988
MET159
4.567
ARG165
3.683
TYR168
3.720
Residue
Distance (Å)
LEU169
3.377
GLN172
3.042
VAL197
3.932
LYS198
2.834
SER199
3.166
ASP200
1.288
THR202
1.338
LEU203
3.422
UNK505
4.553
References  Top
REF 1 Structure-activity relationships and X-ray structures describing the selectivity of aminopyrazole inhibitors for c-Jun N-terminal kinase 3 (JNK3) over p38. J Biol Chem. 2009 May 8;284(19):12853-61.
REF 2 Synthesis, biological evaluation, X-ray structure, and pharmacokinetics of aminopyrimidine c-jun-N-terminal kinase (JNK) inhibitors. J Med Chem. 2010 Jan 14;53(1):419-31.
REF 3 3,5-Disubstituted quinolines as novel c-Jun N-terminal kinase inhibitors. Bioorg Med Chem Lett. 2007 Nov 15;17(22):6378-82.
REF 4 Synthesis and SAR of piperazine amides as novel c-jun N-terminal kinase (JNK) inhibitors. Bioorg Med Chem Lett. 2009 Jun 15;19(12):3344-7.

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