6D2L: Human CARM1 with (S)-SKI-72

Crystal structure of human CARM1 with (S)-SKI-72. Determined by X-ray diffraction at 2.0 Å resolution. Released 23 May 2018.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 6
Atoms: 16,868
Mol. weight: 237.96 kDa
Ligands: FTG
Released: 23 May 2018

Explore 6D2L in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6D2L contains 91 α-helices and 126 β-strands across 6 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: 15 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	151-154	4
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	311-313	3
β-strand	318	1	4
β-strand	321	1	4
α-helix	324-326	3
α-helix	327-335	9
α-helix	338	1
β-strand	339-341	3	3
α-helix	345-347	3
β-strand	348	1	3
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	433-442	10	5
β-strand	448-456	9	5
β-strand	462-468	7	5
β-strand	473-474	2	3

Chain B: 15 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	152-154	3
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
β-strand	339-341	3	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	417-428	12	8
β-strand	433-443	11	10
β-strand	447-456	10	10
β-strand	462-468	7	10
β-strand	473-474	2	8

Chain C: 15 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	149-153	5
α-helix	156-163	8
α-helix	166-177	12
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	311-313	3
β-strand	318	1	14
β-strand	321	1	14
α-helix	324-326	3
α-helix	327-335	9
α-helix	338	1
β-strand	339-341	3	13
α-helix	345-347	3
β-strand	348	1	13
β-strand	353-358	6	13
α-helix	364-368	5
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	433-443	11	15
β-strand	447-456	10	15
β-strand	461-468	8	15
β-strand	473-474	2	13

Chain D: 15 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	152-154	3
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	265-267	3
α-helix	268-274	7
α-helix	275-278	4
β-strand	279-286	8	16
β-strand	289-297	9	18
α-helix	300-308	9
α-helix	311-314	4
β-strand	318	1	19
β-strand	321	1	19
α-helix	324-326	3
α-helix	327-335	9
β-strand	339-341	3	18
α-helix	345-347	3
β-strand	348	1	18
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	417-428	12	18
β-strand	433-442	10	20
β-strand	448-456	9	20
β-strand	462-468	7	20
β-strand	473-474	2	18

Chain E: 16 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	150-153	4
α-helix	156-163	8
α-helix	166-177	12
α-helix	180-182	3
β-strand	187-191	5	21
α-helix	197-204	8
β-strand	209-214	6	21
α-helix	218-228	11
β-strand	235-239	5	21
β-strand	251-256	6	21
β-strand	260	1	22
β-strand	263	1	22
α-helix	265-267	3
α-helix	268-274	7
α-helix	275-278	4
β-strand	279-286	8	21
β-strand	289-297	9	23
α-helix	300-310	11
α-helix	311-313	3
β-strand	318	1	24
β-strand	321	1	24
α-helix	324-326	3
α-helix	327-335	9
α-helix	338	1
β-strand	339-341	3	23
α-helix	345-347	3
β-strand	348	1	23
β-strand	353-358	6	23
α-helix	364-367	4
β-strand	369-377	9	25
β-strand	382-396	15	23
β-strand	401-405	5	23
β-strand	417-428	12	23
β-strand	433-443	11	25
β-strand	447-456	10	25
β-strand	462-468	7	25
β-strand	473-474	2	23

Chain F: 15 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	150-154	5
α-helix	156-163	8
α-helix	166-178	13
α-helix	180-182	3
β-strand	187-191	5	26
α-helix	197-204	8
β-strand	209-214	6	26
α-helix	218-228	11
β-strand	235-239	5	26
α-helix	242-244	3
β-strand	251-256	6	26
β-strand	260	1	27
β-strand	263	1	27
α-helix	268-274	7
α-helix	275-278	4
β-strand	279-286	8	26
β-strand	289-297	9	28
α-helix	300-308	9
α-helix	311-314	4
β-strand	318	1	29
β-strand	321	1	29
α-helix	324-326	3
α-helix	327-335	9
β-strand	339-341	3	28
α-helix	345-347	3
β-strand	348	1	28
β-strand	353-358	6	28
α-helix	364-367	4
β-strand	369-377	9	30
β-strand	382-396	15	28
β-strand	401-405	5	28
β-strand	417-428	12	28
β-strand	433-443	11	30
β-strand	447-456	10	30
β-strand	462-468	7	30
β-strand	473-474	2	28

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone-arginine methyltransferase CARM1	A, B, C, D, E, F	protein	344	Homo sapiens	Q86X55 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F), FASTA

>6D2L_1 Histone-arginine methyltransferase CARM1 (chains A, B, C, D, E, F)
AVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFKDKIVLDVGCGSGILSFFAAQA
GARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVSLPEQVDIIISEPMGYMLFN
ERMLESYLHAKKYLKPSGNMFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSA
LRGAAVDEYFRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGLVH
GLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTLSGTCLLIANKR
QSYDISIVAQVDQTGSKSSNLLDLKNPFFRYTGTTPSPPPGSHY

Ligands and cofactors

ID	Name	Formula	Copies
FTG	(2S,5S)-2-amino-6-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahy…	C31 H40 N8 O5	6

Water and common crystallization additives (SO4, GOL, UNX) are not listed.

Primary citation

A chemical probe of CARM1 alters epigenetic plasticity against breast cancer cell invasion. Cai, X.C., Zhang, T., Kim, E.J. et al. Elife (2019) 8. DOI 10.7554/eLife.47110 · PubMed

Other PDB entries of the same protein (UniProt Q86X55 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8G2H 1.49 Å, Crystal Structure of PRMT4 with Compound YD1113
6DVR 1.54 Å, Crystal structure of human CARM1 with (R)-SKI-72
8SIG 1.78 Å, Crystal Structure of PRMT4 with Compound YD1-288
6S7A 1.86 Å, Crystal structure of CARM1 in complex with inhibitor AA175
8UQH 1.87 Å, X-ray crystal structure of PRMT4 bound to compound YD-1130
5U4X 1.88 Å, Coactivator-associated arginine methyltransferase 1 with TP-064
6ARJ 1.92 Å, Crystal structure of CARM1 with EPZ022302 and SAH
5DX1 1.93 Å, Crystal structure of CARM1, sinefungin, and PABP1 peptide (R455)
5DX8 1.94 Å, Crystal structure of CARM1, sinefungin, and methylated PABP1 peptide (R455)
5DXJ 1.95 Å, Crystal structure of CARM1 and sinefungin
9O6H 1.97 Å, The Structure of PRMT4 in complex with SGC8172
4IKP 2.0 Å, Crystal structure of coactivator-associated arginine methyltransferase 1 with…

Browse structure collections

About this viewer

MolViewer shows 6D2L directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.