Structure of PDB 2y1w Chain C

Receptor sequence
>2y1wC (length=343) Species: 9606 (Homo sapiens) [Search protein sequence]
SVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFK
DKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDR
IVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGN
MFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEY
FRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGLV
HGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTL
SGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYT
3D structure
PDB2y1w Structural Basis for Carm1 Inhibition by Indole and Pyrazole Inhibitors
ChainC
Resolution2.1 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 C Y150 F151 Y154 M163 R169 G193 C194 I198 E215 A216 K242 E244 E258 M269 Y15 F16 Y19 M28 R34 G58 C59 I63 E80 A81 K107 E109 E123 M134
BS02 849 C Y150 F153 Y154 M163 E258 P259 M260 Y262 E267 H415 W416 Q447 Y15 F18 Y19 M28 E123 P124 M125 Y127 E132 H280 W281 Q312 PDBbind-CN: -logKd/Ki=6.33,Kd=0.465uM
BindingDB: IC50=30nM
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:2y1w, PDBe:2y1w, PDBj:2y1w
PDBsum2y1w
PubMed21410432
UniProtQ86X55|CARM1_HUMAN Histone-arginine methyltransferase CARM1 (Gene Name=CARM1)

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