Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T21585 | Target Info | |||
| Target Name | CDC-like kinase 3 (CLK3) | ||||
| Synonyms | Dual specificity protein kinase CLK3 | ||||
| Target Type | Literature-reported Target | ||||
| Gene Name | CLK3 | ||||
| Biochemical Class | Kinase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | TG003 | Ligand Info | |||
| Canonical SMILES | CCN1C2=C(C=CC(=C2)OC)SC1=CC(=O)C | ||||
| InChI | 1S/C13H15NO2S/c1-4-14-11-8-10(16-3)5-6-12(11)17-13(14)7-9(2)15/h5-8H,4H2,1-3H3/b13-7- | ||||
| InChIKey | BGVLELSCIHASRV-QPEQYQDCSA-N | ||||
| PubChem Compound ID | 1893668 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 6YTY CLK3 A319V mutant bound with benzothiazole Tg003 (Cpd 2) | ||||||
| Method | X-ray diffraction | Resolution | 1.76 Å | Mutation | Yes | [1] |
| PDB Sequence |
QSSKRSSRSV
136 EDDKEGHLVC146 RIGDWLQERY156 EIVGNLGEGT166 FGKVVECLDH176 ARGKSQVALK 186 IIRNVGKYRE196 AARLEINVLK206 KIKEKDKENK216 FLCVLMSDWF226 NFHGHMCIAF 236 ELLGKNTFEF246 LKENNFQPYP256 LPHVRHMAYQ266 LCHALRFLHE276 NQLTHTDLKP 286 ENILFVNSEF296 ETLYNEHCEE308 KSVKNTSIRV318 VDFGSATFDH328 EHHTTIVATR 338 HYRPPEVILE348 LGWAQPCDVW358 SIGCILFEYY368 RGFTLFQTHE378 NREHLVMMEK 388 ILGPIPSHMI398 HRTRKQKYFY408 KGGLVWDENS418 SDGRYVKENC428 KPLKSYMLQD 438 SLEHVQLFDL448 MRRMLEFDPA458 QRITLAEALL468 HPFFAGLTPE478 ERS |
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| PDB ID: 6YTW CLK3 bound with benzothiazole Tg003 (Cpd 2) | ||||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [1] |
| PDB Sequence |
SMQSSKRSSR
134 SVEDDKEGHL144 VCRIGDWLQE154 RYEIVGNLGE164 GTFGKVVECL174 DHARGKSQVA 184 LKIIRNVGKY194 REAARLEINV204 LKKIKEKDKE214 NKFLCVLMSD224 WFNFHGHMCI 234 AFELLGKNTF244 EFLKENNFQP254 YPLPHVRHMA264 YQLCHALRFL274 HENQLTHTDL 284 KPENILFVNS294 EFETLEKSVK312 NTSIRVADFG322 SATFDHEHHT332 TIVATRHYRP 342 PEVILELGWA352 QPCDVWSIGC362 ILFEYYRGFT372 LFQTHENREH382 LVMMEKILGP 392 IPSHMIHRTR402 KQKYFYKGGL412 VWDENSSDGR422 YVKENCKPLK432 SYMLQDSLEH 442 VQLFDLMRRM452 LEFDPAQRIT462 LAEALLHPFF472 AGLTPEERS
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | DFG-1 Residue Controls Inhibitor Binding Mode and Affinity, Providing a Basis for Rational Design of Kinase Inhibitor Selectivity. J Med Chem. 2020 Sep 24;63(18):10224-10234. | ||||
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