Structure of PDB 5k8v Chain A Binding Site BS01

Receptor Information
>5k8v Chain A (length=343) Species: 10090 (Mus musculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFK
DKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDR
IVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGN
MFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEY
FRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGLV
HGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTL
SGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYT
Ligand information
Ligand ID6RE
InChIInChI=1S/C12H18N8O3/c13-9-6-10(18-3-17-9)20(4-19-6)11-8(22)7(21)5(23-11)1-2-16-12(14)15/h3-5,7-8,11,21-22H,1-2H2,(H2,13,17,18)(H4,14,15,16)/p+1/t5-,7-,8-,11-/m1/s1
InChIKeyOIGRVZYOOMUALG-IOSLPCCCSA-O
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.5c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CCNC(=[NH2+])N)O)O)N
OpenEye OEToolkits 2.0.5c1nc(c2c(n1)n(cn2)C3C(C(C(O3)CCNC(=[NH2+])N)O)O)N
CACTVS 3.385NC(=[NH2+])NCC[CH]1O[CH]([CH](O)[CH]1O)n2cnc3c(N)ncnc23
CACTVS 3.385NC(=[NH2+])NCC[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23
FormulaC12 H19 N8 O3
Name[[2-[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]ethylamino]-azanyl-methylidene]azanium
ChEMBL
DrugBank
ZINC
PDB chain5k8v Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5k8v Structural studies of protein arginine methyltransferase 2 reveal its interactions with potential substrates and inhibitors.
Resolution2.25 Å
Binding residue
(original residue number in PDB)		Y150 F151 Y154 G193 E215 A216 K242 E244 E258 M260 E267 M269
Binding residue
(residue number reindexed from 1)		Y15 F16 Y19 G58 E80 A81 K107 E109 E123 M125 E132 M134
Annotation score2
Binding affinityMOAD: ic50=460nM
PDBbind-CN: -logKd/Ki=6.34,IC50=460nM
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.
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:5k8v, PDBe:5k8v, PDBj:5k8v
PDBsum5k8v
PubMed27879050
UniProtQ9WVG6|CARM1_MOUSE Histone-arginine methyltransferase CARM1 (Gene Name=Carm1)

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