Structure of PDB 5dx1 Chain C

Receptor sequence
>5dx1C (length=344) Species: 9606 (Homo sapiens) [Search protein sequence]
RSVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDF
KDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTD
RIVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSG
NMFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDE
YFRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGL
VHGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDT
LSGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYT
3D structure
PDB5dx1 Structural Insights into Ternary Complex Formation of Human CARM1 with Various Substrates.
ChainC
Resolution1.93 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D165 E257 E266 H414
Catalytic site (residue number reindexed from 1) D32 E124 E133 H281
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 peptide C F152 N161 E257 M259 Y261 E266 H414 Y416 F474 Y476 F19 N28 E124 M126 Y128 E133 H281 Y283 F341 Y343
BS02 SFG C Y149 F150 Y153 M162 R168 G192 C193 I197 L198 E214 A215 K241 E243 E257 M268 Y16 F17 Y20 M29 R35 G59 C60 I64 L65 E81 A82 K108 E110 E124 M135
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:5dx1, PDBe:5dx1, PDBj:5dx1
PDBsum5dx1
PubMed26551522
UniProtQ86X55|CARM1_HUMAN Histone-arginine methyltransferase CARM1 (Gene Name=CARM1)

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