Structure of PDB 2y1w Chain D

Receptor sequence

>2y1wD (length=343) Species: 9606 (Homo sapiens) [Search protein sequence]

SVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFK
DKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDR
IVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGN
MFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEY
FRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGLV
HGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTL
SGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYT

3D structure

PDB

2y1w Structural Basis for Carm1 Inhibition by Indole and Pyrazole Inhibitors

Chain

Resolution

2.1 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)	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	SFG	D	F151 Y154 Q160 M163 R169 G193 C194 I198 L199 E215 A216 K242 V243 E244 E258 M269 S272	F16 Y19 Q25 M28 R34 G58 C59 I63 L64 E80 A81 K107 V108 E109 E123 M134 S137
BS02	849	D	Q149 Y150 F153 Y154 M163 E258 P259 M260 Y262 E267 H415 W416 Q447	Q14 Y15 F18 Y19 M28 E123 P124 M125 Y127 E132 H280 W281 Q312	BindingDB: IC50=30nM

Gene Ontology

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

	Biological Process
GO:0018216	peptidyl-arginine methylation

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:2y1w, PDBe:2y1w, PDBj:2y1w
PDBsum	2y1w
PubMed	21410432
UniProt	Q86X55\|CARM1_HUMAN Histone-arginine methyltransferase CARM1 (Gene Name=CARM1)

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