Structure of PDB 5dwq Chain C

Receptor sequence
>5dwqC (length=342) Species: 9606 (Homo sapiens) [Search protein sequence]
VFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFKD
KIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRI
VVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGNM
FPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEYF
RQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGLVH
GLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTLS
GTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYT
3D structure
PDB5dwq Structural Insights into Ternary Complex Formation of Human CARM1 with Various Substrates.
ChainC
Resolution2.36 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) D30 E122 E131 H279
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 Y149 F150 Y153 M162 R168 G192 C193 I197 E214 A215 K241 V242 E243 M268 Y14 F15 Y18 M27 R33 G57 C58 I62 E79 A80 K106 V107 E108 M133
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:5dwq, PDBe:5dwq, PDBj:5dwq
PDBsum5dwq
PubMed26551522
UniProtQ86X55|CARM1_HUMAN Histone-arginine methyltransferase CARM1 (Gene Name=CARM1)

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