Structure of PDB 5lgr Chain C

Receptor sequence

>5lgrC (length=344) Species: 10090 (Mus musculus)

RSVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDF
KDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTD
RIVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSG
NMFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDE
YFRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGL
VHGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDT
LSGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYT

3D structure

• PDB: 5lgr Transition state mimics are valuable mechanistic probes for structural studies with the arginine methyltransferase CARM1.
• Chain: C
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D166 E258 E267 H415
• Catalytic site (residue number reindexed from 1): D32 E124 E133 H281
• 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	C	F153 Y154 N162 M163 E258 M260 Y262 E267 H415 Y417 F475	F19 Y20 N28 M29 E124 M126 Y128 E133 H281 Y283 F341
BS02	peptide	C	S158 Q159 Y477	S24 Q25 Y343
BS03	LPD	C	L413 T414 Y417	L279 T280 Y283
BS04	QVR	C	Y150 F151 Y154 G193 E215 A216 K242 E244 E258 M269	Y16 F17 Y20 G59 E81 A82 K108 E110 E124 M135

Gene Ontology

Molecular Function

• GO:0016274 protein-arginine N-methyltransferase activity

Biological Process

• GO:0018216 peptidyl-arginine methylation

External links

• PDB: RCSB:5lgr, PDBe:5lgr, PDBj:5lgr
• PDBsum: 5lgr
• PubMed: 28330993
• UniProt: Q9WVG6|CARM1_MOUSE Histone-arginine methyltransferase CARM1 (Gene Name=Carm1)