Structure of PDB 5dx0 Chain D

Receptor sequence

>5dx0D (length=343) Species: 9606 (Homo sapiens)

SVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFK
DKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDR
IVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGN
MFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEY
FRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGLV
HGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTL
SGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYT

3D structure

• PDB: 5dx0 Structural Insights into Ternary Complex Formation of Human CARM1 with Various Substrates.
• Chain: D
• Resolution: 2.05 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D165 E257 E266 H414
• 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	D	F152 Y153 N161 D165 E257 M259 Y261 N265 E266 H414 Y416	F18 Y19 N27 D31 E123 M125 Y127 N131 E132 H280 Y282
BS02	SFG	D	Y149 F150 Y153 Q159 M162 R168 G192 C193 I197 L198 E214 A215 K241 V242 E243 E257 M268	Y15 F16 Y19 Q25 M28 R34 G58 C59 I63 L64 E80 A81 K107 V108 E109 E123 M134

Gene Ontology

Molecular Function

• GO:0016274 protein-arginine N-methyltransferase activity

Biological Process

• GO:0018216 peptidyl-arginine methylation

External links

• PDB: RCSB:5dx0, PDBe:5dx0, PDBj:5dx0
• PDBsum: 5dx0
• PubMed: 26551522
• UniProt: Q86X55|CARM1_HUMAN Histone-arginine methyltransferase CARM1 (Gene Name=CARM1)