Crystal structure of CARM1 with EPZ022302 and SAH. Determined by X-ray diffraction at 1.92 Å resolution. Released 7 Feb 2018.
Explore 6ARJ in 3D Show helices and sheets RCSB PDB PDBe
6ARJ contains 64 α-helices and 84 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 | 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 | 311-314 | 4 | |
| 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 | 1 | 3 |
| 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 | 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 | |
| β-strand | 339-340 | 2 | 8 |
| α-helix | 345-347 | 3 | |
| β-strand | 348 | 1 | 8 |
| α-helix | 351-352 | 2 | |
| β-strand | 353-358 | 6 | 8 |
| α-helix | 364-367 | 4 | |
| β-strand | 369-377 | 9 | 10 |
| β-strand | 382-396 | 15 | 8 |
| β-strand | 401-405 | 5 | 8 |
| β-strand | 418-428 | 11 | 8 |
| β-strand | 433-443 | 11 | 10 |
| β-strand | 447-456 | 10 | 10 |
| β-strand | 462-468 | 7 | 10 |
| β-strand | 473 | 1 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 136-140 | 5 | |
| α-helix | 143-154 | 12 | |
| α-helix | 156-163 | 8 | |
| α-helix | 166-178 | 13 | |
| α-helix | 180-182 | 3 | |
| β-strand | 187-191 | 5 | 11 |
| α-helix | 197-204 | 8 | |
| β-strand | 209-214 | 6 | 11 |
| α-helix | 218-228 | 11 | |
| β-strand | 235-239 | 5 | 11 |
| β-strand | 251-256 | 6 | 11 |
| β-strand | 260 | 1 | 12 |
| β-strand | 263 | 1 | 12 |
| α-helix | 268-274 | 7 | |
| α-helix | 275-278 | 4 | |
| β-strand | 279-286 | 8 | 11 |
| β-strand | 289-297 | 9 | 13 |
| α-helix | 300-310 | 11 | |
| α-helix | 311-314 | 4 | |
| β-strand | 318 | 1 | 14 |
| β-strand | 321 | 1 | 14 |
| α-helix | 324-326 | 3 | |
| α-helix | 327-335 | 9 | |
| β-strand | 339-341 | 3 | 13 |
| α-helix | 345-347 | 3 | |
| β-strand | 348 | 1 | 13 |
| α-helix | 351-352 | 2 | |
| β-strand | 353-358 | 6 | 13 |
| α-helix | 364-367 | 4 | |
| β-strand | 369-377 | 9 | 15 |
| β-strand | 382-396 | 15 | 13 |
| β-strand | 401-405 | 5 | 13 |
| β-strand | 417-428 | 12 | 13 |
| β-strand | 433-442 | 10 | 15 |
| β-strand | 448-456 | 9 | 15 |
| β-strand | 461-468 | 8 | 15 |
| β-strand | 473 | 1 | 13 |
| 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 | 16 |
| α-helix | 197-204 | 8 | |
| β-strand | 209-214 | 6 | 16 |
| α-helix | 218-228 | 11 | |
| β-strand | 235-239 | 5 | 16 |
| β-strand | 251-256 | 6 | 16 |
| β-strand | 260 | 1 | 17 |
| β-strand | 263 | 1 | 17 |
| α-helix | 268-274 | 7 | |
| α-helix | 275-278 | 4 | |
| β-strand | 279-286 | 8 | 16 |
| β-strand | 289-297 | 9 | 18 |
| α-helix | 300-310 | 11 | |
| α-helix | 311-313 | 3 | |
| β-strand | 318 | 1 | 19 |
| β-strand | 321 | 1 | 19 |
| α-helix | 324-326 | 3 | |
| α-helix | 327-335 | 9 | |
| β-strand | 339-340 | 2 | 18 |
| α-helix | 345-347 | 3 | |
| β-strand | 348 | 1 | 18 |
| α-helix | 351-352 | 2 | |
| β-strand | 353-358 | 6 | 18 |
| α-helix | 364-367 | 4 | |
| β-strand | 369-377 | 9 | 20 |
| β-strand | 382-396 | 15 | 18 |
| β-strand | 401-405 | 5 | 18 |
| β-strand | 418-428 | 11 | 18 |
| β-strand | 433-443 | 11 | 20 |
| β-strand | 447-456 | 10 | 20 |
| β-strand | 462-468 | 7 | 20 |
| β-strand | 473 | 1 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone-arginine methyltransferase CARM1 | A, B, C, D | protein | 349 | Homo sapiens | Q86X55 (AlphaFold model) |
>6ARJ_1 Histone-arginine methyltransferase CARM1 (chains A, B, C, D) SIARSVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFKDKIVLD VGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVSLPEQ VDIIISEPMGYMLFNERMLESYLHAKKYLKPSGNMFPTIGDVHLAPFTDEQLYMEQFTKA NFWYQPSFHGVDLSALRGAAVDEYFRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRI EIPFKFHMLHSGLVHGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKA GDTLSGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYTGT
| ID | Name | Formula | Copies |
|---|---|---|---|
| BW4 | methyl 2-[2-{2-chloro-5-[(2R)-2-hydroxy-3-(methylamino)propoxy]phenyl}-6-(3,5-d… | C29 H37 Cl N6 O5 | 4 |
| SAH | S-adenosyl-L-homocysteine | C14 H20 N6 O5 S | 4 |
Water and common crystallization additives (SO4, GOL) are not listed.
Identification of a CARM1 Inhibitor with Potent In Vitro and In Vivo Activity in Preclinical Models of Multiple Myeloma. Drew, A.E., Moradei, O., Jacques, S.L. et al. Sci Rep (2017) 7:17993-17993. DOI 10.1038/s41598-017-18446-z · 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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