Structure of PDB 3b3f Chain B

Receptor sequence
>3b3fB (length=337) Species: 10116 (Rattus norvegicus) [Search protein sequence]
TEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFKDKIVLD
VGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPG
KVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGNMFPTIG
DVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEYFRQPVV
DTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGLVHGLAFW
FDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTLSGTCLL
IANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYT
3D structure
PDB3b3f Functional insights from structures of coactivator-associated arginine methyltransferase 1 domains.
ChainB
Resolution2.2 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 B Y150 F151 Y154 M163 R169 G193 C194 I198 E215 A216 K242 M269 S272 Y9 F10 Y13 M22 R28 G52 C53 I57 E74 A75 K101 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
External links
PDB RCSB:3b3f, PDBe:3b3f, PDBj:3b3f
PDBsum3b3f
PubMed17882262
UniProtQ4AE70|CARM1_RAT Histone-arginine methyltransferase CARM1 (Gene Name=Carm1)

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