Structure of PDB 6s74 Chain C

Receptor sequence
>6s74C (length=342) Species: 9606 (Homo sapiens) [Search protein sequence]
SVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFK
DKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDR
IVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGN
MFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEY
FRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGLV
HGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTL
SGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRY
3D structure
PDB6s74 Structural and biochemical evaluation of bisubstrate inhibitors of protein arginine N-methyltransferases PRMT1 and CARM1 (PRMT4).
ChainC
Resolution2.1 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 2.1.1.319: type I protein arginine methyltransferase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 KY8 C Y149 F150 Y153 R168 G192 E214 A215 K241 E243 E257 M259 Y261 E266 M268 W415 Y15 F16 Y19 R34 G58 E80 A81 K107 E109 E123 M125 Y127 E132 M134 W281 MOAD: Kd=2.3uM
Gene Ontology
Molecular Function
GO:0016274 protein-arginine N-methyltransferase activity
Biological Process
GO:0018216 peptidyl-arginine methylation

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:6s74, PDBe:6s74, PDBj:6s74
PDBsum6s74
PubMed32011657
UniProtQ86X55|CARM1_HUMAN Histone-arginine methyltransferase CARM1 (Gene Name=CARM1)

[Back to BioLiP]