Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T12837 | Target Info | |||
| Target Name | Histone-arginine methyltransferase CARM1 (CARM1) | ||||
| Synonyms | Protein arginine N-methyltransferase 4; PRMT4; Histonearginine methyltransferase CARM1; Coactivatorassociated arginine methyltransferase 1; Coactivator-associated arginine methyltransferase 1 | ||||
| Target Type | Literature-reported Target | ||||
| Gene Name | CARM1 | ||||
| Biochemical Class | Methyltransferase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | Sinefungin | Ligand Info | |||
| Canonical SMILES | C1=NC(=C2C(=N1)N(C=N2)C3C(C(C(O3)CC(CCC(C(=O)O)N)N)O)O)N | ||||
| InChI | 1S/C15H23N7O5/c16-6(1-2-7(17)15(25)26)3-8-10(23)11(24)14(27-8)22-5-21-9-12(18)19-4-20-13(9)22/h4-8,10-11,14,23-24H,1-3,16-17H2,(H,25,26)(H2,18,19,20)/t6-,7-,8+,10+,11+,14+/m0/s1 | ||||
| InChIKey | LMXOHSDXUQEUSF-YECHIGJVSA-N | ||||
| PubChem Compound ID | 65482 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 5DX1 Crystal structure of CARM1, sinefungin, and PABP1 peptide (R455) | ||||||
| Method | X-ray diffraction | Resolution | 1.93 Å | Mutation | Yes | [1] |
| PDB Sequence |
RSVFSERTEE
143 SSAVQYFQFY153 GYLSQQQNMM163 QDYVRTGTYQ173 RAILQNHTDF183 KDKIVLDVGC 193 GSGILSFFAA203 QAGARKIYAV213 EASTMAQHAE223 VLVKSNNLTD233 RIVVIPGKVE 243 EVSLPEQVDI253 IISEPMGYML263 FNERMLESYL273 HAKKYLKPSG283 NMFPTIGDVH 293 LAPFTDEQLY303 MEQFTKANFW313 YQPSFHGVDL323 SALRGAAVDE333 YFRQPVVDTF 343 DIRILMAKSV353 KYTVNFLEAK363 EGDLHRIEIP373 FKFHMLHSGL383 VHGLAFWFDV 393 AFIGSIMTVW403 LSTAPTEPLT413 HWYQVRCLFQ423 SPLFAKAGDT433 LSGTCLLIAN 443 KRQSYDISIV453 AQVDQTGSKS463 SNLLDLKNPF473 FRYT
|
|||||
|
|
PHE137
3.798
TYR149
3.498
PHE150
3.659
TYR153
3.451
GLN159
3.239
MET162
3.447
MET163
4.562
ARG168
2.636
ASP190
4.235
VAL191
4.547
GLY192
2.884
CYS193
3.398
GLY194
3.634
SER195
4.778
|
|||||
| PDB ID: 5DX8 Crystal structure of CARM1, sinefungin, and methylated PABP1 peptide (R455) | ||||||
| Method | X-ray diffraction | Resolution | 1.94 Å | Mutation | Yes | [1] |
| PDB Sequence |
RSVFSERTEE
143 SSAVQYFQFY153 GYLSQQQNMM163 QDYVRTGTYQ173 RAILQNHTDF183 KDKIVLDVGC 193 GSGILSFFAA203 QAGARKIYAV213 EASTMAQHAE223 VLVKSNNLTD233 RIVVIPGKVE 243 EVSLPEQVDI253 IISEPMGYML263 FNERMLESYL273 HAKKYLKPSG283 NMFPTIGDVH 293 LAPFTDEQLY303 MEQFTKANFW313 YQPSFHGVDL323 SALRGAAVDE333 YFRQPVVDTF 343 DIRILMAKSV353 KYTVNFLEAK363 EGDLHRIEIP373 FKFHMLHSGL383 VHGLAFWFDV 393 AFIGSIMTVW403 LSTAPTEPLT413 HWYQVRCLFQ423 SPLFAKAGDT433 LSGTCLLIAN 443 KRQSYDISIV453 AQVDQTGSKS463 SNLLDLKNPF473 FRYT
|
|||||
|
|
PHE137
3.990
TYR149
3.615
PHE150
3.587
TYR153
3.366
GLN159
3.219
MET162
3.405
MET163
4.500
ARG168
2.600
ASP190
4.344
VAL191
4.486
GLY192
2.886
CYS193
3.383
GLY194
3.652
SER195
4.820
|
|||||
| PDB ID: 5DXJ Crystal structure of CARM1 and sinefungin | ||||||
| Method | X-ray diffraction | Resolution | 1.95 Å | Mutation | No | [1] |
| PDB Sequence |
RSVFSERTEE
143 SSAVQYFQFY153 GYLSQQQNMM163 QDYVRTGTYQ173 RAILQNHTDF183 KDKIVLDVGC 193 GSGILSFFAA203 QAGARKIYAV213 EASTMAQHAE223 VLVKSNNLTD233 RIVVIPGKVE 243 EVSLPEQVDI253 IISEPMGYML263 FNERMLESYL273 HAKKYLKPSG283 NMFPTIGDVH 293 LAPFTDEQLY303 MEQFTKANFW313 YQPSFHGVDL323 SALRGAAVDE333 YFRQPVVDTF 343 DIRILMAKSV353 KYTVNFLEAK363 EGDLHRIEIP373 FKFHMLHSGL383 VHGLAFWFDV 393 AFIGSIMTVW403 LSTAPTEPLT413 HWYQVRCLFQ423 SPLFAKAGDT433 LSGTCLLIAN 443 KRQSYDISIV453 AQVDQTGSKS463 SNLLDLKNPF473 FRYT
|
|||||
|
|
PHE137
4.025
TYR149
3.435
PHE150
3.591
TYR153
3.379
GLN159
3.230
MET162
3.422
MET163
4.541
ARG168
2.665
ASP190
4.237
VAL191
4.713
GLY192
2.879
CYS193
3.327
GLY194
3.669
SER195
4.670
|
|||||
| PDB ID: 5DX0 Crystal structure of CARM1, sinefungin, and H3 peptide (R17) | ||||||
| Method | X-ray diffraction | Resolution | 2.05 Å | Mutation | Yes | [1] |
| PDB Sequence |
SVFSERTEES
144 SAVQYFQFYG154 YLSQQQNMMQ164 DYVRTGTYQR174 AILQNHTDFK184 DKIVLDVGCG 194 SGILSFFAAQ204 AGARKIYAVE214 ASTMAQHAEV224 LVKSNNLTDR234 IVVIPGKVEE 244 VSLPEQVDII254 ISEPMGYMLF264 NERMLESYLH274 AKKYLKPSGN284 MFPTIGDVHL 294 APFTDEQLYM304 EQFTKANFWY314 QPSFHGVDLS324 ALRGAAVDEY334 FRQPVVDTFD 344 IRILMAKSVK354 YTVNFLEAKE364 GDLHRIEIPF374 KFHMLHSGLV384 HGLAFWFDVA 394 FIGSIMTVWL404 STAPTEPLTH414 WYQVRCLFQS424 PLFAKAGDTL434 SGTCLLIANK 444 RQSYDISIVA454 QVDQTGSKSS464 NLLDLKNPFF474 RYT
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .SFG or .SFG2 or .SFG3 or :3SFG;style chemicals stick;color identity;select .A:137 or .A:149 or .A:150 or .A:153 or .A:159 or .A:162 or .A:163 or .A:168 or .A:190 or .A:191 or .A:192 or .A:193 or .A:194 or .A:195 or .A:197 or .A:198 or .A:213 or .A:214 or .A:215 or .A:216 or .A:240 or .A:241 or .A:242 or .A:243 or .A:257 or .A:268 or .A:271; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
PHE137
4.050
TYR149
3.440
PHE150
3.393
TYR153
3.234
GLN159
3.373
MET162
3.204
MET163
4.484
ARG168
2.815
ASP190
4.122
VAL191
4.357
GLY192
2.974
CYS193
3.337
GLY194
3.725
SER195
4.652
|
|||||
| PDB ID: 5DXA Crystal structure of CARM1, sinefungin, and methylated PABP1 peptide (R460) | ||||||
| Method | X-ray diffraction | Resolution | 2.07 Å | Mutation | Yes | [1] |
| PDB Sequence |
RSVFSERTEE
143 SSAVQYFQFY153 GYLSQQQNMM163 QDYVRTGTYQ173 RAILQNHTDF183 KDKIVLDVGC 193 GSGILSFFAA203 QAGARKIYAV213 EASTMAQHAE223 VLVKSNNLTD233 RIVVIPGKVE 243 EVSLPEQVDI253 IISEPMGYML263 FNERMLESYL273 HAKKYLKPSG283 NMFPTIGDVH 293 LAPFTDEQLY303 MEQFTKANFW313 YQPSFHGVDL323 SALRGAAVDE333 YFRQPVVDTF 343 DIRILMAKSV353 KYTVNFLEAK363 EGDLHRIEIP373 FKFHMLHSGL383 VHGLAFWFDV 393 AFIGSIMTVW403 LSTAPTEPLT413 HWYQVRCLFQ423 SPLFAKAGDT433 LSGTCLLIAN 443 KRQSYDISIV453 AQVDQTGSKS463 SNLLDLKNPF473 FRYT
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .SFG or .SFG2 or .SFG3 or :3SFG;style chemicals stick;color identity;select .A:137 or .A:149 or .A:150 or .A:153 or .A:159 or .A:162 or .A:163 or .A:168 or .A:190 or .A:191 or .A:192 or .A:193 or .A:194 or .A:195 or .A:197 or .A:198 or .A:213 or .A:214 or .A:215 or .A:216 or .A:240 or .A:241 or .A:242 or .A:243 or .A:257 or .A:258 or .A:268 or .A:271; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
PHE137
3.927
TYR149
3.639
PHE150
3.563
TYR153
3.253
GLN159
2.981
MET162
3.359
MET163
4.468
ARG168
2.814
ASP190
4.312
VAL191
4.585
GLY192
2.951
CYS193
3.198
GLY194
3.732
SER195
4.810
|
|||||
| PDB ID: 5DWQ Crystal structure of CARM1, sinefungin, and methylated H3 peptide (R17) | ||||||
| Method | X-ray diffraction | Resolution | 2.36 Å | Mutation | Yes | [1] |
| PDB Sequence |
SVFSERTEES
144 SAVQYFQFYG154 YLSQQQNMMQ164 DYVRTGTYQR174 AILQNHTDFK184 DKIVLDVGCG 194 SGILSFFAAQ204 AGARKIYAVE214 ASTMAQHAEV224 LVKSNNLTDR234 IVVIPGKVEE 244 VSLPEQVDII254 ISEPMGYMLF264 NERMLESYLH274 AKKYLKPSGN284 MFPTIGDVHL 294 APFTDEQLYM304 EQFTKANFWY314 QPSFHGVDLS324 ALRGAAVDEY334 FRQPVVDTFD 344 IRILMAKSVK354 YTVNFLEAKE364 GDLHRIEIPF374 KFHMLHSGLV384 HGLAFWFDVA 394 FIGSIMTVWL404 STAPTEPLTH414 WYQVRCLFQS424 PLFAKAGDTL434 SGTCLLIANK 444 RQSYDISIVA454 QVDQTGSKSS464 NLLDLKNPFF474 RY
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .SFG or .SFG2 or .SFG3 or :3SFG;style chemicals stick;color identity;select .A:137 or .A:149 or .A:150 or .A:153 or .A:159 or .A:162 or .A:163 or .A:168 or .A:190 or .A:191 or .A:192 or .A:193 or .A:194 or .A:195 or .A:197 or .A:198 or .A:213 or .A:214 or .A:215 or .A:216 or .A:240 or .A:241 or .A:242 or .A:243 or .A:257 or .A:268 or .A:271; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
PHE137
3.798
TYR149
3.492
PHE150
3.634
TYR153
3.376
GLN159
3.393
MET162
3.329
MET163
4.685
ARG168
2.878
ASP190
4.368
VAL191
4.554
GLY192
2.778
CYS193
3.136
GLY194
3.685
SER195
4.796
|
|||||
| PDB ID: 2Y1W CRYSTAL STRUCTURE OF COACTIVATOR ASSOCIATED ARGININE METHYLTRANSFERASE 1 (CARM1) IN COMPLEX WITH SINEFUNGIN AND INDOLE INHIBITOR | ||||||
| Method | X-ray diffraction | Resolution | 2.10 Å | Mutation | No | [2] |
| PDB Sequence |
SVFSERTEES
145 SAVQYFQFYG155 YLSQQQNMMQ165 DYVRTGTYQR175 AILQNHTDFK185 DKIVLDVGCG 195 SGILSFFAAQ205 AGARKIYAVE215 ASTMAQHAEV225 LVKSNNLTDR235 IVVIPGKVEE 245 VSLPEQVDII255 ISEPMGYMLF265 NERMLESYLH275 AKKYLKPSGN285 MFPTIGDVHL 295 APFTDEQLYM305 EQFTKANFWY315 QPSFHGVDLS325 ALRGAAVDEY335 FRQPVVDTFD 345 IRILMAKSVK355 YTVNFLEAKE365 GDLHRIEIPF375 KFHMLHSGLV385 HGLAFWFDVA 395 FIGSIMTVWL405 STAPTEPLTH415 WYQVRCLFQS425 PLFAKAGDTL435 SGTCLLIANK 445 RQSYDISIVA455 QVDQTGSKSS465 NLLDLKNPFF475 RYTG
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .SFG or .SFG2 or .SFG3 or :3SFG;style chemicals stick;color identity;select .A:138 or .A:150 or .A:151 or .A:154 or .A:160 or .A:163 or .A:164 or .A:169 or .A:191 or .A:192 or .A:193 or .A:194 or .A:195 or .A:196 or .A:198 or .A:199 or .A:214 or .A:215 or .A:216 or .A:217 or .A:241 or .A:242 or .A:243 or .A:244 or .A:258 or .A:259 or .A:269 or .A:272; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
PHE138
4.048
TYR150
3.681
PHE151
3.451
TYR154
3.244
GLN160
2.966
MET163
3.490
MET164
4.548
ARG169
2.839
ASP191
4.127
VAL192
4.661
GLY193
2.913
CYS194
3.162
GLY195
3.635
SER196
4.678
|
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Structural Insights into Ternary Complex Formation of Human CARM1 with Various Substrates. ACS Chem Biol. 2016 Mar 18;11(3):763-71. | ||||
| REF 2 | Structural basis for CARM1 inhibition by indole and pyrazole inhibitors. Biochem J. 2011 Jun 1;436(2):331-9. | ||||
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