Structure of PDB 2y1x Chain A

Receptor sequence
>2y1xA (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
ChainA
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 A 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 BindingDB: Ki=400nM
BS02 845 A F153 Y154 N162 M163 E258 M260 Y262 E267 H415 W416 F475 F18 Y19 N27 M28 E123 M125 Y127 E132 H280 W281 F340
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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