BioLiP

Structure of PDB 3b3f Chain C

Receptor sequence

>3b3fC (length=337) Species: 10116 (Rattus norvegicus) [Search protein sequence]

TEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFKDKIVLD
VGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPG
KVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGNMFPTIG
DVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEYFRQPVV
DTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGLVHGLAFW
FDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTLSGTCLL
IANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYT

3D structure

PDB

3b3f Functional insights from structures of coactivator-associated arginine methyltransferase 1 domains.

Chain

Resolution

2.2 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	D166 E258 E267 H415
Catalytic site (residue number reindexed from 1)	D25 E117 E126 H274
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	SAH	C	Y150 F151 Y154 Q160 M163 R169 G193 C194 I198 E215 A216 K242 V243 E244 E258 M269 S272	Y9 F10 Y13 Q19 M22 R28 G52 C53 I57 E74 A75 K101 V102 E103 E117 M128 S131

Gene Ontology

	Molecular Function
GO:0016274	protein-arginine N-methyltransferase activity

	Biological Process
GO:0018216	peptidyl-arginine methylation

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Molecular Function

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Biological Process

PDB	RCSB:3b3f, PDBe:3b3f, PDBj:3b3f
PDBsum	3b3f
PubMed	17882262
UniProt	Q4AE70\|CARM1_RAT Histone-arginine methyltransferase CARM1 (Gene Name=Carm1)