Structure of PDB 7os4 Chain D

Receptor sequence
>7os4D (length=343) Species: 10090 (Mus musculus) [Search protein sequence]
SVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFK
DKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDR
IVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGN
MFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEY
FRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGLV
HGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTL
SGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYT
3D structure
PDB7os4 Structural Studies Provide New Insights into the Role of Lysine Acetylation on Substrate Recognition by CARM1 and Inform the Design of Potent Peptidomimetic Inhibitors.
ChainD
Resolution2.54 Å
3D
structure
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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 peptide D F153 Y154 Q159 N162 E258 Y262 N266 E267 L413 H415 Y417 K471 F475 F18 Y19 Q24 N27 E123 Y127 N131 E132 L278 H280 Y282 K336 F340
BS02 QVR D Y150 F151 Y154 G193 E215 A216 E258 E267 M269 Y15 F16 Y19 G58 E80 A81 E123 E132 M134
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:7os4, PDBe:7os4, PDBj:7os4
PDBsum7os4
PubMed34569136
UniProtQ9WVG6|CARM1_MOUSE Histone-arginine methyltransferase CARM1 (Gene Name=Carm1)

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