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 T91761 Target Info
Target Name T-cell-specific kinase (ITK)
Synonyms Tyrosine kinase ITK; Inducible T cell kinase; EMT
Target Type Clinical trial Target
Gene Name ITK
Biochemical Class Kinase
UniProt ID
ITK_HUMAN
Ligand General Information  Top
Ligand Name 4-(Carbamoylamino)-1-[7-(Propan-2-Yloxy)naphthalen-1-Yl]-1h-Pyrazole-3-Carboxamide Ligand Info
Canonical SMILES CC(C)OC1=CC2=C(C=CC=C2N3C=C(C(=N3)C(=O)N)NC(=O)N)C=C1
InChI 1S/C18H19N5O3/c1-10(2)26-12-7-6-11-4-3-5-15(13(11)8-12)23-9-14(21-18(20)25)16(22-23)17(19)24/h3-10H,1-2H3,(H2,19,24)(H3,20,21,25)
InChIKey GYKHVLWAQGEZTM-UHFFFAOYSA-N
PubChem Compound ID 73386655
Drug Binding Sites of Target  Top
PDB ID: 4M15      Crystal structure of ITK in complex with compound 9 [4-(carbamoylamino)-1-[7-(propan-2-yloxy)naphthalen-1-yl]-1H-pyrazole-3-carboxamide] and ADP
Method X-ray diffraction Resolution 1.52 Å Mutation No [1]
PDB Sequence
KWVIDPSELT
364
FVQEIGSGQF
374
GLVHLGYWLN
384
KDKVAIKTIR
394
EGAMSEEDFI
404

EEAEVMMKLS
414
HPKLVQLYGV
424
CLEQAPICLV
434
FEFMEHGCLS
444
DYLRTQRGLF
454

AAETLLGMCL
464
DVCEGMAYLE
474
EACVIHRDLA
484
ARNCLVGENQ
494
VIKVSDFGMT
504

RFVLDDQYTS
514
STGTKFPVKW
524
ASPEVFSFSR
534
YSSKSDVWSF
544
GVLMWEVFSE
554

GKIPYENRSN
564
SEVVEDISTG
574
FRLYKPRLAS
584
THVYQIMNHC
594
WRERPEDRPA
604

FSRLLRQLAE
614
IAE
Residue
Distance (Å)
TRP356
3.999
PHE403
3.324
GLU406
3.690
ALA407
3.560
MET410
2.812
MET411
3.557
LEU413
3.656
VAL419
2.776
GLN420
3.579
LEU421
2.956
TYR422
4.345
Residue
Distance (Å)
GLY423
3.713
VAL424
4.240
PHE435
3.640
VAL498
4.419
SER499
2.934
ASP500
2.862
PHE501
3.111
GLY502
4.341
MET503
4.678
ARG505
3.970
PHE506
3.538
PDB ID: 4M14      Crystal structure of ITK in complex with compound 9 [4-(carbamoylamino)-1-[7-(propan-2-yloxy)naphthalen-1-yl]-1H-pyrazole-3-carboxamide]
Method X-ray diffraction Resolution 1.55 Å Mutation No [1]
PDB Sequence
KWVIDPSELT
364
FVQEIGSGQF
374
GLVHLGYWLN
384
KDKVAIKTIR
394
EGAMSEEDFI
404

EEAEVMMKLS
414
HPKLVQLYGV
424
CLEQAPICLV
434
FEFMEHGCLS
444
DYLRTQRGLF
454

AAETLLGMCL
464
DVCEGMAYLE
474
EACVIHRDLA
484
ARNCLVGENQ
494
VIKVSDFGMT
504

RFVLDDQYTS
514
STGTKFPVKW
524
ASPEVFSFSR
534
YSSKSDVWSF
544
GVLMWEVFSE
554

GKIPYENRSN
564
SEVVEDISTG
574
FRLYKPRLAS
584
THVYQIMNHC
594
WRERPEDRPA
604

FSRLLRQLAE
614
IAE
Residue
Distance (Å)
TRP356
3.969
ILE369
3.183
GLY370
3.911
SER371
3.907
GLY372
4.328
VAL377
3.787
ALA389
3.336
LYS391
2.869
PHE403
3.268
GLU406
3.642
ALA407
3.443
MET410
2.762
MET411
3.515
LEU413
3.655
VAL419
2.796
GLN420
3.568
LEU421
2.943
TYR422
4.374
GLY423
3.711
Residue
Distance (Å)
VAL424
4.109
PHE435
3.676
GLU436
2.898
PHE437
3.592
MET438
2.800
GLU439
3.414
HIS440
4.435
GLY441
3.509
CYS442
4.075
LEU489
3.504
VAL498
4.402
SER499
2.936
ASP500
2.922
PHE501
3.114
GLY502
4.421
MET503
4.689
ARG505
4.018
PHE506
3.511
References  Top
REF 1 Selectively targeting an inactive conformation of interleukin-2-inducible T-cell kinase by allosteric inhibitors. Biochem J. 2014 Jun 1;460(2):211-22.

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