8UQH: PRMT4

X-ray crystal structure of PRMT4 bound to compound YD-1130. Determined by X-ray diffraction at 1.87 Å resolution. Released 2 Apr 2025.

Method
X-ray diffraction
Resolution
1.87 Å
Organism
Homo sapiens
Chains
4
Atoms
12,191
Mol. weight
157.08 kDa
Ligands
X9L
Released
2 Apr 2025

Explore 8UQH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8UQH contains 59 α-helices and 90 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: 16 helices, 23 β-strands

ElementResiduesLengthSheet
α-helix143-15412
α-helix157-1648
α-helix167-17812
α-helix181-1833
β-strand18511
β-strand188-19252
α-helix198-2058
β-strand20811
β-strand210-21562
α-helix219-22911
β-strand236-24052
β-strand252-25762
α-helix262-2643
α-helix269-2757
α-helix276-2794
β-strand280-28782
β-strand290-29893
α-helix301-31111
α-helix312-3143
β-strand31914
β-strand32214
α-helix325-3273
α-helix328-3369
β-strand340-34233
α-helix346-3483
β-strand34913
β-strand35115
α-helix352-3532
β-strand354-35963
α-helix365-3684
β-strand370-37896
β-strand37915
β-strand383-397153
β-strand402-40653
β-strand418-429123
β-strand434-443106
β-strand449-45796
β-strand463-46976
β-strand474-47523
Chain B: 13 helices, 23 β-strands
ElementResiduesLengthSheet
α-helix144-15310
α-helix157-1648
α-helix167-17812
α-helix181-1833
β-strand188-19257
α-helix198-2058
β-strand210-21567
α-helix219-22911
β-strand236-24057
β-strand252-25767
β-strand26118
β-strand26418
α-helix269-2757
α-helix276-2794
β-strand280-28787
β-strand290-29899
α-helix301-31111
β-strand319110
β-strand322110
α-helix325-3273
α-helix328-3369
β-strand340-34239
α-helix346-3483
β-strand34919
β-strand351111
β-strand354-35969
α-helix365-3684
β-strand370-378912
β-strand379111
β-strand383-397159
β-strand402-40659
β-strand418-429129
β-strand434-4431012
β-strand449-457912
β-strand463-469712
β-strand474-47529
Chain C: 15 helices, 21 β-strands
ElementResiduesLengthSheet
α-helix143-15412
α-helix157-1648
α-helix167-17913
α-helix181-1833
β-strand188-192513
α-helix198-2058
β-strand210-215613
α-helix219-22911
β-strand236-240513
β-strand252-257613
β-strand261114
β-strand264114
α-helix269-2757
α-helix276-2794
β-strand280-287813
β-strand290-298915
α-helix301-31111
α-helix312-3154
β-strand319116
β-strand322116
α-helix325-3273
α-helix328-3369
β-strand340-342315
α-helix346-3483
β-strand349115
α-helix352-3532
β-strand354-359615
α-helix365-3695
β-strand370-378917
β-strand383-3971515
β-strand402-406515
β-strand418-4291215
β-strand434-4441117
β-strand448-4571017
β-strand462-469817
β-strand474-475215
Chain D: 15 helices, 23 β-strands
ElementResiduesLengthSheet
α-helix143-15412
α-helix157-1648
α-helix167-17812
α-helix181-1833
β-strand188-192518
α-helix198-2058
β-strand210-215618
α-helix219-22911
β-strand236-240518
β-strand252-257618
β-strand261119
β-strand264119
α-helix269-2757
α-helix276-2794
β-strand280-287818
β-strand290-298920
α-helix301-31212
α-helix313-3153
β-strand319121
β-strand322121
α-helix325-3273
α-helix328-3369
β-strand340-342320
α-helix346-3483
β-strand349120
β-strand351122
α-helix352-3532
β-strand354-359620
α-helix365-3684
β-strand370-378923
β-strand379122
β-strand383-3971520
β-strand402-406520
β-strand418-4291220
β-strand434-4441123
β-strand448-4571023
β-strand462-469823
β-strand474-475220

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Histone-arginine methyltransferase CARM1A, B, C, Dprotein341Homo sapiensQ86X55 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>8UQH_1 Histone-arginine methyltransferase CARM1 (chains A, B, C, D)
ERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFKDKIVLDVGCGSGIL
SFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVSLPEQVDIIISEP
MGYMLFNERMLESYLHAKKYLKPSGNMFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSF
HGVDLSALRGAAVDEYFRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHM
LHSGLVHGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTLSGTC
LLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYTGT

Ligands and cofactors

IDNameFormulaCopies
X9L5'-S-(2-{[(3-bromophenyl)methyl]amino}ethyl)-5'-thioadenosineC19 H23 Br N6 O3 S4

Primary citation

An Adenosine Analogue Library Reveals Insights into Active Sites of Protein Arginine Methyltransferases and Enables the Discovery of a Selective PRMT4 Inhibitor. Deng, Y., Kim, E.J., Song, X. et al. J Med Chem (2024) 67:18053-18069. DOI 10.1021/acs.jmedchem.4c01041 · 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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