Structure of PDB 5lgp Chain A

Receptor sequence

>5lgpA (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: A
• 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	A	Q149 Y150 F153 Y154 N162 M163 E258 M260 Y262 E267 H415 Y417 F474 F475	Q14 Y15 F18 Y19 N27 M28 E123 M125 Y127 E132 H280 Y282 F339 F340
BS02	peptide	A	Y156 S158 Q159 F475	Y21 S23 Q24 F340
BS03	8ZB	A	Y150 F151 Y154 G193 E215 A216 K242 V243 E244 E258 E267 M269	Y15 F16 Y19 G58 E80 A81 K107 V108 E109 E123 E132 M134
BS04	LPD	A	T414 Y417	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)