Structure of PDB 5dx1 Chain D

Receptor sequence

>5dx1D (length=344) Species: 9606 (Homo sapiens)

RSVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDF
KDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTD
RIVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSG
NMFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDE
YFRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGL
VHGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDT
LSGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYT

3D structure

• PDB: 5dx1 Structural Insights into Ternary Complex Formation of Human CARM1 with Various Substrates.
• Chain: D
• Resolution: 1.93 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D165 E257 E266 H414
• 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	D	F152 Y153 N161 M162 E257 M259 Y261 E266 L412 H414 Y416 F474 Y476	F19 Y20 N28 M29 E124 M126 Y128 E133 L279 H281 Y283 F341 Y343
BS02	SFG	D	Y149 F150 Y153 Q159 M162 R168 G192 C193 I197 E214 A215 K241 V242 E243 E257 M268	Y16 F17 Y20 Q26 M29 R35 G59 C60 I64 E81 A82 K108 V109 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:5dx1, PDBe:5dx1, PDBj:5dx1
• PDBsum: 5dx1
• PubMed: 26551522
• UniProt: Q86X55|CARM1_HUMAN Histone-arginine methyltransferase CARM1 (Gene Name=CARM1)