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 | (4~{S})-7,8-bis(chloranyl)-9-methyl-1-oxidanylidene-spiro[2,4-dihydropyrido[3,4-b]indole-3,4'-piperidine]-4-carbonitrile | Ligand Info | |||
| Canonical SMILES | CN1C2=C(C=CC(=C2Cl)Cl)C3=C1C(=O)NC4(C3C#N)CCNCC4 | ||||
| InChI | 1S/C17H16Cl2N4O/c1-23-14-9(2-3-11(18)13(14)19)12-10(8-20)17(4-6-21-7-5-17)22-16(24)15(12)23/h2-3,10,21H,4-7H2,1H3,(H,22,24)/t10-/m0/s1 | ||||
| InChIKey | OWAWOKKHZNRHGV-JTQLQIEISA-N | ||||
| PubChem Compound ID | 124504856 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 6YU1 CLK3 bound with beta-carboline KH-CARB13 (Cpd 3) | ||||||
| Method | X-ray diffraction | Resolution | 1.90 Å | Mutation | No | [1] |
| PDB Sequence |
SVEDDKEGHL
144 VCRIGDWLQE154 RYEIVGNLGE164 GTFGKVVECL174 DHARGKSQVA184 LKIIRNVGKY 194 REAARLEINV204 LKKIKEKDKE214 NKFLCVLMSD224 WFNFHGHMCI234 AFELLGKNTF 244 EFLKENNFQP254 YPLPHVRHMA264 YQLCHALRFL274 HENQLTHTDL284 KPENILFVNS 294 EFETLYEKSV311 KNTSIRVADF321 GSATFDHEHH331 TTIVATRHYR341 PPEVILELGW 351 AQPCDVWSIG361 CILFEYYRGF371 TLFQTHENRE381 HLVMMEKILG391 PIPSHMIHRT 401 RKQKYFYKGG411 LVWDENSSDG421 RYVKENCKPL431 KSYMLQDSLE441 HVQLFDLMRR 451 MLEFDPAQRI461 TLAEALLHPF471 FAGLTPEERS481
|
|||||
|
|
||||||
| PDB ID: 6Z2V CLK3 A319V mutant bound with beta-carboline KH-CARB13 (Cpd 3) | ||||||
| Method | X-ray diffraction | Resolution | 2.60 Å | Mutation | Yes | [1] |
| PDB Sequence |
RSVEDDKEGH
143 LVCRIGDWLQ153 ERYEIVGNLG163 EGTFGKVVEC173 LDHARGKSQV183 ALKIIRNVGK 193 YREAARLEIN203 VLKKIKEKDK213 ENKFLCVLMS223 DWFNFHGHMC233 IAFELLGKNT 243 FEFLKENNFQ253 PYPLPHVRHM263 AYQLCHALRF273 LHENQLTHTD283 LKPENILFVN 293 SEFETLEKSV311 KNTSIRVVDF321 GSATFDHEHH331 TTIVATRHYR341 PPEVILELGW 351 AQPCDVWSIG361 CILFEYYRGF371 TLFQTHENRE381 HLVMMEKILG391 PIPSHMIHRT 401 RKQKYFYKGG411 LVWDENSSDG421 RYVKENCKPL431 KSYMLQDSLE441 HVQLFDLMRR 451 MLEFDPAQRI461 TLAEALLHPF471 FAGLTPEER
|
|||||
|
|
||||||
| 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. | ||||
If You Find Any Error in Data or Bug in Web Service, Please Kindly Report It to Dr. Zhou and Dr. Zhang.