Structure of PDB 5lgr Chain D Binding Site BS02

Receptor Information
>5lgr Chain D (length=343) Species: 10090 (Mus musculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RSVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDF
KDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTD
RIVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSG
NMFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDE
YFRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGL
VHGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDT
LSGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRY
Ligand information
Ligand IDQVR
InChIInChI=1S/C12H15N5O3/c1-2-3-6-8(18)9(19)12(20-6)17-5-16-7-10(13)14-4-15-11(7)17/h2-6,8-9,12,18-19H,1H3,(H2,13,14,15)/b3-2+/t6-,8-,9-,12-/m1/s1
InChIKeyUYHMWDPUDJRZGB-JVINVVEESA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.6C/C=C/[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)O)O
OpenEye OEToolkits 2.0.6CC=CC1C(C(C(O1)n2cnc3c2ncnc3N)O)O
CACTVS 3.385CC=C[CH]1O[CH]([CH](O)[CH]1O)n2cnc3c(N)ncnc23
CACTVS 3.385C/C=C/[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23
FormulaC12 H15 N5 O3
Name(2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-[(~{E})-prop-1-enyl]oxolane-3,4-diol
ChEMBL
DrugBank
ZINC
PDB chain5lgr Chain H Residue 102 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB5lgr Transition state mimics are valuable mechanistic probes for structural studies with the arginine methyltransferase CARM1.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		Y150 F151 Y154 G193 E215 A216 E244 E258 M269
Binding residue
(residue number reindexed from 1)		Y16 F17 Y20 G59 E81 A82 E110 E124 M135
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) D166 E258 E267 H415
Catalytic site (residue number reindexed from 1) D32 E124 E133 H281
Enzyme Commision number 2.1.1.319: type I protein arginine methyltransferase.
Gene Ontology
Molecular Function
GO:0016274 protein-arginine N-methyltransferase activity
Biological Process
GO:0018216 peptidyl-arginine methylation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5lgr, PDBe:5lgr, PDBj:5lgr
PDBsum5lgr
PubMed28330993
UniProtQ9WVG6|CARM1_MOUSE Histone-arginine methyltransferase CARM1 (Gene Name=Carm1)

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