6S74: CARM1

Crystal structure of CARM1 in complex with inhibitor UM305. Determined by X-ray diffraction at 2.1 Å resolution. Released 4 Mar 2020.

Method
X-ray diffraction
Resolution
2.1 Å
Organism
Homo sapiens
Chains
4
Atoms
11,804
Mol. weight
162.2 kDa
Ligands
KY8
Released
4 Mar 2020

Explore 6S74 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 17 helices, 21 β-strands

ElementResiduesLengthSheet
α-helix136-1405
α-helix143-15311
α-helix156-1638
α-helix166-17813
α-helix180-1823
β-strand187-19151
α-helix197-2048
β-strand209-21461
α-helix218-22811
β-strand235-23951
β-strand251-25661
β-strand26012
β-strand26312
α-helix265-2673
α-helix268-2747
α-helix275-2784
β-strand279-28681
β-strand289-29793
α-helix300-31011
α-helix311-3133
β-strand31814
β-strand32114
α-helix324-3263
α-helix327-3359
β-strand339-34133
α-helix345-3473
β-strand34813
α-helix351-3522
β-strand353-35863
α-helix364-3674
β-strand369-37795
β-strand382-396153
β-strand401-40553
β-strand417-428123
β-strand433-443115
β-strand447-456105
β-strand461-46885
β-strand473-47423
Chain B: 17 helices, 23 β-strands
ElementResiduesLengthSheet
α-helix136-1405
α-helix143-15311
α-helix156-1638
α-helix166-17813
α-helix180-1823
β-strand187-19156
α-helix197-2048
β-strand209-21466
α-helix218-22811
β-strand235-23956
β-strand251-25666
β-strand26017
β-strand26317
α-helix268-2747
α-helix275-2784
β-strand279-28686
β-strand289-29798
α-helix300-31011
α-helix311-3133
β-strand31819
β-strand32119
α-helix324-3263
α-helix327-3359
α-helix3381
β-strand339-34138
α-helix345-3473
β-strand34818
β-strand350110
α-helix351-3522
β-strand353-35868
α-helix364-3674
β-strand369-377911
β-strand378110
β-strand382-396158
β-strand401-40558
β-strand417-428128
β-strand433-4431111
β-strand447-4561011
β-strand462-468711
β-strand473-47428
Chain C: 17 helices, 21 β-strands
ElementResiduesLengthSheet
α-helix136-1405
α-helix143-15311
α-helix156-1638
α-helix166-17712
α-helix180-1823
β-strand187-191512
α-helix197-2048
β-strand209-214612
α-helix218-22811
β-strand235-239512
β-strand251-256612
β-strand260113
β-strand263113
α-helix265-2673
α-helix268-2747
α-helix275-2784
β-strand279-286812
β-strand289-297914
α-helix300-31011
α-helix311-3144
β-strand318115
β-strand321115
α-helix324-3263
α-helix327-3359
β-strand339-341314
α-helix345-3473
β-strand348114
α-helix351-3522
β-strand353-358614
α-helix364-3674
β-strand369-377916
β-strand382-3961514
β-strand401-405514
β-strand417-4281214
β-strand433-4431116
β-strand447-4561016
β-strand461-468816
β-strand473-474214
Chain D: 16 helices, 21 β-strands
ElementResiduesLengthSheet
α-helix136-1405
α-helix143-15311
α-helix156-1638
α-helix166-17813
α-helix180-1823
β-strand187-191517
α-helix197-2048
β-strand209-214617
α-helix218-22811
β-strand235-239517
β-strand251-256617
β-strand260118
β-strand263118
α-helix268-2747
α-helix275-2784
β-strand279-286817
β-strand289-297919
α-helix300-31011
α-helix311-3144
β-strand318120
β-strand321120
α-helix324-3263
α-helix327-33610
β-strand339-341319
α-helix345-3473
β-strand348119
α-helix351-3522
β-strand353-358619
α-helix364-3674
β-strand369-377921
β-strand382-3961519
β-strand401-405519
β-strand417-4281219
β-strand433-4431121
β-strand447-4561021
β-strand461-468821
β-strand473-474219

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Histone-arginine methyltransferase CARM1A, B, C, Dprotein351Homo sapiensQ86X55 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>6S74_1 Histone-arginine methyltransferase CARM1 (chains A, B, C, D)
SVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFKDKIVLDVGCG
SGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVSLPEQVDII
ISEPMGYMLFNERMLESYLHAKKYLKPSGNMFPTIGDVHLAPFTDEQLYMEQFTKANFWY
QPSFHGVDLSALRGAAVDEYFRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPF
KFHMLHSGLVHGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTL
SGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYTGTHHHHHH

Ligands and cofactors

IDNameFormulaCopies
KY8(2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-[[3-azanylpropyl-[3-(pyrimidi…C20 H30 N10 O34

Water and common crystallization additives (GOL) are not listed.

Primary citation

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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