Structure of PDB 5lgq Chain C

Receptor sequence
>5lgqC (length=343) Species: 10090 (Mus musculus) [Search protein sequence]
SVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFK
DKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDR
IVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGN
MFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEY
FRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGLV
HGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTL
SGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYT
3D structure
PDB5lgq Transition state mimics are valuable mechanistic probes for structural studies with the arginine methyltransferase CARM1.
ChainC
Resolution2.11 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 peptide C F153 Y154 N162 M163 E258 M260 Y262 E267 T414 H415 Y417 F475 F18 Y19 N27 M28 E123 M125 Y127 E132 T279 H280 Y282 F340
BS02 8ZB C Y150 F151 Y154 G193 E215 A216 E244 E258 M269 Y15 F16 Y19 G58 E80 A81 E109 E123 M134
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:5lgq, PDBe:5lgq, PDBj:5lgq
PDBsum5lgq
PubMed28330993
UniProtQ9WVG6|CARM1_MOUSE Histone-arginine methyltransferase CARM1 (Gene Name=Carm1)

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