Structure of PDB 2v74 Chain D

Receptor sequence
>2v74D (length=332) Species: 10090 (Mus musculus) [Search protein sequence]
VQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFKDKIVLDVGCGSG
ILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVS
LPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGNMFPTIGDVHLAP
FTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEYFRQPVVDTFDIR
ILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGLVHGLAFWFDVAFI
GSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTLSGTCLLIANKRQ
SYDISIVAQVDQTGSKSSNLLDLKNPFFRYTG
3D structure
PDB2v74 Insights Into Histone Code Syntax from Structural and Biochemical Studies of Carm1 Methyltransferase
ChainD
Resolution2.7 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) D19 E111 E120 H268
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 D F151 Y154 Q160 M163 R169 G193 C194 I198 L199 E215 A216 K242 M269 S272 F4 Y7 Q13 M16 R22 G46 C47 I51 L52 E68 A69 K95 M122 S125
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:2v74, PDBe:2v74, PDBj:2v74
PDBsum2v74
PubMed17882261
UniProtQ9WVG6|CARM1_MOUSE Histone-arginine methyltransferase CARM1 (Gene Name=Carm1)

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