Structure of PDB 2y1x Chain B

Receptor sequence
>2y1xB (length=342) Species: 9606 (Homo sapiens) [Search protein sequence]
SVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFK
DKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDR
IVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGN
MFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEY
FRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGLV
HGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTL
SGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRY
3D structure
PDB2y1x Structural Basis for Carm1 Inhibition by Indole and Pyrazole Inhibitors
ChainB
Resolution2.4 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 SAH B F151 Y154 M163 R169 G193 C194 I198 L199 E215 A216 K242 E244 E258 M269 F16 Y19 M28 R34 G58 C59 I63 L64 E80 A81 K107 E109 E123 M134 BindingDB: Ki=400nM
BS02 845 B F153 Y154 N162 M163 E258 P259 M260 Y262 E267 H415 W416 F475 F18 Y19 N27 M28 E123 P124 M125 Y127 E132 H280 W281 F340 PDBbind-CN: -logKd/Ki=7.57,IC50=0.027uM
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:2y1x, PDBe:2y1x, PDBj:2y1x
PDBsum2y1x
PubMed21410432
UniProtQ86X55|CARM1_HUMAN Histone-arginine methyltransferase CARM1 (Gene Name=CARM1)

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