Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T82665 | Target Info | |||
| Target Name | Protein arginine methyltransferase 5 (PRMT5) | ||||
| Synonyms | Shk1 kinase-binding protein 1 homolog; SKB1Hs; SKB1 homolog; SKB1; Protein arginine N-methyltransferase 5; Jak-binding protein 1; JBP1; IBP72; Histone-arginine N-methyltransferase PRMT5; HRMT1L5; 72 kDa ICln-binding protein | ||||
| Target Type | Clinical trial Target | ||||
| Gene Name | PRMT5 | ||||
| Biochemical Class | Methyltransferase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | EPZ015666 | Ligand Info | |||
| Canonical SMILES | C1CN(CC2=CC=CC=C21)CC(CNC(=O)C3=CC(=NC=N3)NC4COC4)O | ||||
| InChI | 1S/C20H25N5O3/c26-17(10-25-6-5-14-3-1-2-4-15(14)9-25)8-21-20(27)18-7-19(23-13-22-18)24-16-11-28-12-16/h1-4,7,13,16-17,26H,5-6,8-12H2,(H,21,27)(H,22,23,24)/t17-/m0/s1 | ||||
| InChIKey | ZKXZLIFRWWKZRY-KRWDZBQOSA-N | ||||
| PubChem Compound ID | 90241673 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 4X60 Crystal structure of PRMT5:MEP50 with EPZ015666 and sinefungin | ||||||
| Method | X-ray diffraction | Resolution | 2.35 Å | Mutation | No | [1] |
| PDB Sequence |
RVSSGRDLNC
22 VPEIADTLGA32 VAKQGFDFLC42 MPVFHPRFKR52 EFIQEPAKNR62 PGPQTRSDLL 72 LSGRDWNTLI82 VGKLSPWIRP92 DSKVEKIRRN102 SEAAMLQELN112 FGAYLGLPAF 122 LLPLNQEDNT132 NLARVLTNHI142 HTGHHSSMFW152 MRVPLVAPED162 LRDDIIENAP 172 TTHTEEYSGE182 EKTWMWWHNF192 RTLCDYSKRI202 AVALEIGADL212 PSNHVIDRWL 222 GEPIKAAILP232 TSIFLTNKKG242 FPVLSKMHQR252 LIFRLLKLEV262 QFIITGTNHH 272 SEKEFCSYLQ282 YLEYLSQNRP292 PPNAYELFAK302 GYEDYLQSPL312 QPLMDNLESQ 322 TYEVFEKDPI332 KYSQYQQAIY342 KCLLDRVPEE352 EKDTNVQVLM362 VLGAGRGPLV 372 NASLRAAKQA382 DRRIKLYAVE392 KNPNAVVTLE402 NWQFEEWGSQ412 VTVVSSDMRE 422 WVAPEKADII432 VSELLGSFAD442 NELSPECLDG452 AQHFLKDDGV462 SIPGEYTSFL 472 APISSSKLYN482 EVRACREKDR492 DPEAQFEMPY502 VVRLHNFHQL512 SAPQPCFTFS 522 HPNRDPMIDN532 NRYCTLEFPV542 EVNTVLHGFA552 GYFETVLYQD562 ITLSIRPETH 572 SPGMFSWFPI582 LFPIKQPITV592 REGQTICVRF602 WRCSNSKKVW612 YEWAVTAPVC 622 SAIHNPTGRS632 YTIGL
|
|||||
|
|
PHE300
3.797
ALA301
4.607
TYR304
3.826
GLN309
3.426
LEU312
4.293
LEU319
3.661
THR323
4.364
TYR324
4.097
VAL326
4.228
PHE327
3.483
LYS333
3.639
|
|||||
| PDB ID: 4X61 Crystal structure of PRMT5:MEP50 with EPZ015666 and SAM | ||||||
| Method | X-ray diffraction | Resolution | 2.85 Å | Mutation | No | [1] |
| PDB Sequence |
RVSSGRDLNC
22 VPEIADTLGA32 VAKQGFDFLC42 MPVFHPRFKR52 EFIQEPAKNR62 PGPQTRSDLL 72 LSGRDWNTLI82 VGKLSPWIRP92 DSKVEKIRRN102 SEAAMLQELN112 FGAYLGLPAF 122 LLPLNQEDNT132 NLARVLTNHI142 HTGHHSSMFW152 MRVPLVAPED162 LRDDIIENAP 172 TTHTEEYSGE182 EKTWMWWHNF192 RTLCDYSKRI202 AVALEIGADL212 PSNHVIDRWL 222 GEPIKAAILP232 TSIFLTNKKG242 FPVLSKMHQR252 LIFRLLKLEV262 QFIITGTNHH 272 SEKEFCSYLQ282 YLEYLSQNRP292 PPNAYELFAK302 GYEDYLQSPL312 QPLMDNLESQ 322 TYEVFEKDPI332 KYSQYQQAIY342 KCLLDRVPEE352 EKDTNVQVLM362 VLGAGRGPLV 372 NASLRAAKQA382 DRRIKLYAVE392 KNPNAVVTLE402 NWQFEEWGSQ412 VTVVSSDMRE 422 WVAPEKADII432 VSELLGSFAD442 NELSPECLDG452 AQHFLKDDGV462 SIPGEYTSFL 472 APISSSKLYN482 EVRACREKDR492 DPEAQFEMPY502 VVRLHNFHQL512 SAPQPCFTFS 522 HPNRDPMIDN532 NRYCTLEFPV542 EVNTVLHGFA552 GYFETVLYQD562 ITLSIRPETH 572 SPGMFSWFPI582 LFPIKQPITV592 REGQTICVRF602 WRCSNSKKVW612 YEWAVTAPVC 622 SAIHNPTGRS632 YTIGL
|
|||||
|
|
PHE300
3.818
ALA301
4.604
TYR304
3.779
GLN309
3.661
LEU319
3.554
THR323
4.388
TYR324
3.953
VAL326
3.966
PHE327
3.542
LYS333
3.741
TYR334
4.509
|
|||||
| PDB ID: 4X63 Crystal structure of PRMT5:MEP50 with EPZ015666 and SAH | ||||||
| Method | X-ray diffraction | Resolution | 3.05 Å | Mutation | No | [1] |
| PDB Sequence |
RVSSGRDLNC
22 VPEIADTLGA32 VAKQGFDFLC42 MPVFHPRFKR52 EFIQEPAKNR62 PGPQTRSDLL 72 LSGRDWNTLI82 VGKLSPWIRP92 DSKVEKIRRN102 SEAAMLQELN112 FGAYLGLPAF 122 LLPLNQEDNT132 NLARVLTNHI142 HTGHHSSMFW152 MRVPLVAPED162 LRDDIIENAP 172 TTHTEEYSGE182 EKTWMWWHNF192 RTLCDYSKRI202 AVALEIGADL212 PSNHVIDRWL 222 GEPIKAAILP232 TSIFLTNKKG242 FPVLSKMHQR252 LIFRLLKLEV262 QFIITGTNHH 272 SEKEFCSYLQ282 YLEYLSQNRP292 PPNAYELFAK302 GYEDYLQSPL312 QPLMDNLESQ 322 TYEVFEKDPI332 KYSQYQQAIY342 KCLLDRVPEE352 EKDTNVQVLM362 VLGAGRGPLV 372 NASLRAAKQA382 DRRIKLYAVE392 KNPNAVVTLE402 NWQFEEWGSQ412 VTVVSSDMRE 422 WVAPEKADII432 VSELLGSFAD442 NELSPECLDG452 AQHFLKDDGV462 SIPGEYTSFL 472 APISSSKLYN482 EVRACREKDR492 DPEAQFEMPY502 VVRLHNFHQL512 SAPQPCFTFS 522 HPNRDPMIDN532 NRYCTLEFPV542 EVNTVLHGFA552 GYFETVLYQD562 ITLSIRPETH 572 SPGMFSWFPI582 LFPIKQPITV592 REGQTICVRF602 WRCSNSKKVW612 YEWAVTAPVC 622 SAIHNPTGRS632 YTIGL
|
|||||
|
|
PHE300
3.834
ALA301
4.782
TYR304
3.791
GLN309
3.112
LEU312
3.831
LEU319
3.739
THR323
4.502
TYR324
3.952
VAL326
3.996
PHE327
3.492
LYS333
3.511
|
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | A selective inhibitor of PRMT5 with in vivo and in vitro potency in MCL models. Nat Chem Biol. 2015 Jun;11(6):432-7. | ||||
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