Crystal structure of CARM1 in complex with inhibitor UM305. Determined by X-ray diffraction at 2.1 Å resolution. Released 4 Mar 2020.
Explore 6S74 in 3D Show helices and sheets RCSB PDB PDBe
6S74 contains 67 α-helices and 86 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 136-140 | 5 | |
| α-helix | 143-153 | 11 | |
| α-helix | 156-163 | 8 | |
| α-helix | 166-178 | 13 | |
| α-helix | 180-182 | 3 | |
| β-strand | 187-191 | 5 | 1 |
| α-helix | 197-204 | 8 | |
| β-strand | 209-214 | 6 | 1 |
| α-helix | 218-228 | 11 | |
| β-strand | 235-239 | 5 | 1 |
| β-strand | 251-256 | 6 | 1 |
| β-strand | 260 | 1 | 2 |
| β-strand | 263 | 1 | 2 |
| α-helix | 265-267 | 3 | |
| α-helix | 268-274 | 7 | |
| α-helix | 275-278 | 4 | |
| β-strand | 279-286 | 8 | 1 |
| β-strand | 289-297 | 9 | 3 |
| α-helix | 300-310 | 11 | |
| α-helix | 311-313 | 3 | |
| β-strand | 318 | 1 | 4 |
| β-strand | 321 | 1 | 4 |
| α-helix | 324-326 | 3 | |
| α-helix | 327-335 | 9 | |
| β-strand | 339-341 | 3 | 3 |
| α-helix | 345-347 | 3 | |
| β-strand | 348 | 1 | 3 |
| α-helix | 351-352 | 2 | |
| β-strand | 353-358 | 6 | 3 |
| α-helix | 364-367 | 4 | |
| β-strand | 369-377 | 9 | 5 |
| β-strand | 382-396 | 15 | 3 |
| β-strand | 401-405 | 5 | 3 |
| β-strand | 417-428 | 12 | 3 |
| β-strand | 433-443 | 11 | 5 |
| β-strand | 447-456 | 10 | 5 |
| β-strand | 461-468 | 8 | 5 |
| β-strand | 473-474 | 2 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 136-140 | 5 | |
| α-helix | 143-153 | 11 | |
| α-helix | 156-163 | 8 | |
| α-helix | 166-178 | 13 | |
| α-helix | 180-182 | 3 | |
| β-strand | 187-191 | 5 | 6 |
| α-helix | 197-204 | 8 | |
| β-strand | 209-214 | 6 | 6 |
| α-helix | 218-228 | 11 | |
| β-strand | 235-239 | 5 | 6 |
| β-strand | 251-256 | 6 | 6 |
| β-strand | 260 | 1 | 7 |
| β-strand | 263 | 1 | 7 |
| α-helix | 268-274 | 7 | |
| α-helix | 275-278 | 4 | |
| β-strand | 279-286 | 8 | 6 |
| β-strand | 289-297 | 9 | 8 |
| α-helix | 300-310 | 11 | |
| α-helix | 311-313 | 3 | |
| β-strand | 318 | 1 | 9 |
| β-strand | 321 | 1 | 9 |
| α-helix | 324-326 | 3 | |
| α-helix | 327-335 | 9 | |
| α-helix | 338 | 1 | |
| β-strand | 339-341 | 3 | 8 |
| α-helix | 345-347 | 3 | |
| β-strand | 348 | 1 | 8 |
| β-strand | 350 | 1 | 10 |
| α-helix | 351-352 | 2 | |
| β-strand | 353-358 | 6 | 8 |
| α-helix | 364-367 | 4 | |
| β-strand | 369-377 | 9 | 11 |
| β-strand | 378 | 1 | 10 |
| β-strand | 382-396 | 15 | 8 |
| β-strand | 401-405 | 5 | 8 |
| β-strand | 417-428 | 12 | 8 |
| β-strand | 433-443 | 11 | 11 |
| β-strand | 447-456 | 10 | 11 |
| β-strand | 462-468 | 7 | 11 |
| β-strand | 473-474 | 2 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 136-140 | 5 | |
| α-helix | 143-153 | 11 | |
| α-helix | 156-163 | 8 | |
| α-helix | 166-177 | 12 | |
| α-helix | 180-182 | 3 | |
| β-strand | 187-191 | 5 | 12 |
| α-helix | 197-204 | 8 | |
| β-strand | 209-214 | 6 | 12 |
| α-helix | 218-228 | 11 | |
| β-strand | 235-239 | 5 | 12 |
| β-strand | 251-256 | 6 | 12 |
| β-strand | 260 | 1 | 13 |
| β-strand | 263 | 1 | 13 |
| α-helix | 265-267 | 3 | |
| α-helix | 268-274 | 7 | |
| α-helix | 275-278 | 4 | |
| β-strand | 279-286 | 8 | 12 |
| β-strand | 289-297 | 9 | 14 |
| α-helix | 300-310 | 11 | |
| α-helix | 311-314 | 4 | |
| β-strand | 318 | 1 | 15 |
| β-strand | 321 | 1 | 15 |
| α-helix | 324-326 | 3 | |
| α-helix | 327-335 | 9 | |
| β-strand | 339-341 | 3 | 14 |
| α-helix | 345-347 | 3 | |
| β-strand | 348 | 1 | 14 |
| α-helix | 351-352 | 2 | |
| β-strand | 353-358 | 6 | 14 |
| α-helix | 364-367 | 4 | |
| β-strand | 369-377 | 9 | 16 |
| β-strand | 382-396 | 15 | 14 |
| β-strand | 401-405 | 5 | 14 |
| β-strand | 417-428 | 12 | 14 |
| β-strand | 433-443 | 11 | 16 |
| β-strand | 447-456 | 10 | 16 |
| β-strand | 461-468 | 8 | 16 |
| β-strand | 473-474 | 2 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 136-140 | 5 | |
| α-helix | 143-153 | 11 | |
| α-helix | 156-163 | 8 | |
| α-helix | 166-178 | 13 | |
| α-helix | 180-182 | 3 | |
| β-strand | 187-191 | 5 | 17 |
| α-helix | 197-204 | 8 | |
| β-strand | 209-214 | 6 | 17 |
| α-helix | 218-228 | 11 | |
| β-strand | 235-239 | 5 | 17 |
| β-strand | 251-256 | 6 | 17 |
| β-strand | 260 | 1 | 18 |
| β-strand | 263 | 1 | 18 |
| α-helix | 268-274 | 7 | |
| α-helix | 275-278 | 4 | |
| β-strand | 279-286 | 8 | 17 |
| β-strand | 289-297 | 9 | 19 |
| α-helix | 300-310 | 11 | |
| α-helix | 311-314 | 4 | |
| β-strand | 318 | 1 | 20 |
| β-strand | 321 | 1 | 20 |
| α-helix | 324-326 | 3 | |
| α-helix | 327-336 | 10 | |
| β-strand | 339-341 | 3 | 19 |
| α-helix | 345-347 | 3 | |
| β-strand | 348 | 1 | 19 |
| α-helix | 351-352 | 2 | |
| β-strand | 353-358 | 6 | 19 |
| α-helix | 364-367 | 4 | |
| β-strand | 369-377 | 9 | 21 |
| β-strand | 382-396 | 15 | 19 |
| β-strand | 401-405 | 5 | 19 |
| β-strand | 417-428 | 12 | 19 |
| β-strand | 433-443 | 11 | 21 |
| β-strand | 447-456 | 10 | 21 |
| β-strand | 461-468 | 8 | 21 |
| β-strand | 473-474 | 2 | 19 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone-arginine methyltransferase CARM1 | A, B, C, D | protein | 351 | Homo sapiens | Q86X55 (AlphaFold model) |
>6S74_1 Histone-arginine methyltransferase CARM1 (chains A, B, C, D) SVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFKDKIVLDVGCG SGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVSLPEQVDII ISEPMGYMLFNERMLESYLHAKKYLKPSGNMFPTIGDVHLAPFTDEQLYMEQFTKANFWY QPSFHGVDLSALRGAAVDEYFRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPF KFHMLHSGLVHGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTL SGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYTGTHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| KY8 | (2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-[[3-azanylpropyl-[3-(pyrimidi… | C20 H30 N10 O3 | 4 |
Water and common crystallization additives (GOL) are not listed.
Structural and biochemical evaluation of bisubstrate inhibitors of protein arginine N-methyltransferases PRMT1 and CARM1 (PRMT4). Gunnell, E.A., Al-Noori, A., Muhsen, U. et al. Biochem J (2020) 477:787-800. DOI 10.1042/BCJ20190826 · PubMed
Other PDB entries of the same protein (UniProt Q86X55 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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