Structure of PDB 5dwq Chain D

Receptor sequence

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

SVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFK
DKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDR
IVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGN
MFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEY
FRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGLV
HGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTL
SGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYT

3D structure

• PDB: 5dwq Structural Insights into Ternary Complex Formation of Human CARM1 with Various Substrates.
• Chain: D
• Resolution: 2.36 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	Q148 F152 Y153 N161 D165 E257 P258 M259 Y261 E266 H414 Y416 F474	Q14 F18 Y19 N27 D31 E123 P124 M125 Y127 E132 H280 Y282 F340
BS02	SFG	D	Y149 Y153 M162 R168 G192 C193 I197 L198 E214 A215 K241 V242 E243 E257 M268 S271	Y15 Y19 M28 R34 G58 C59 I63 L64 E80 A81 K107 V108 E109 E123 M134 S137

Gene Ontology

Molecular Function

• GO:0016274 protein-arginine N-methyltransferase activity

Biological Process

• GO:0018216 peptidyl-arginine methylation

External links

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