Structure of PDB 5lgp Chain C

Receptor sequence

>5lgpC (length=343) Species: 10090 (Mus musculus)

SVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFK
DKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDR
IVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGN
MFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEY
FRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGLV
HGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTL
SGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYT

3D structure

• PDB: 5lgp Transition state mimics are valuable mechanistic probes for structural studies with the arginine methyltransferase CARM1.
• Chain: C
• Resolution: 2.04 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D166 E258 E267 H415
• Catalytic site (residue number reindexed from 1): D31 E123 E132 H280
• 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	Q149 Y150 F153 Y154 N162 M163 E258 M260 Y262 E267 K310 Y335 Q338 H415 Y417 F474 F475	Q14 Y15 F18 Y19 N27 M28 E123 M125 Y127 E132 K175 Y200 Q203 H280 Y282 F339 F340
BS02	peptide	C	S158 Q159	S23 Q24
BS03	8ZB	C	Y150 F151 Y154 G193 E215 A216 E244 E258 M269	Y15 F16 Y19 G58 E80 A81 E109 E123 M134
BS04	LPD	C	L413 T414 Y417	L278 T279 Y282

Gene Ontology

Molecular Function

• GO:0016274 protein-arginine N-methyltransferase activity

Biological Process

• GO:0018216 peptidyl-arginine methylation

External links

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