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Structure of PDB 5ntc Chain C Binding Site BS02

Receptor Information
>5ntc Chain C (length=348) Species: 10090 (Mus musculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFKDKIVLDVGCGS
GILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPGKVEEV
SLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGNMFPTIGDVHLA
PFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEYFRQPVVDTFDI
RILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGLVHGLAFWFDVAF
IGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTLSGTCLLIANKR
QSYDISIVAQVDQTGSKSSNLLDLKNPFFRYTGTTPSPPPGSHYTSPS
Ligand information
Ligand ID6L7
InChIInChI=1S/C16H26N8O5/c17-2-4-23(3-1-8(18)16(27)28)5-9-11(25)12(26)15(29-9)24-7-22-10-13(19)20-6-21-14(10)24/h6-9,11-12,15,25-26H,1-5,17-18H2,(H,27,28)(H2,19,20,21)/p+3/t8-,9+,11+,12+,15+/m0/s1
InChIKeyRPXXFSOUEYJZLT-OPYVMVOTSA-Q
SMILES
SoftwareSMILES
CACTVS 3.385Nc1ncnc2n(cnc12)[CH]3O[CH](C[NH+](CC[NH3+])CC[CH]([NH3+])C(O)=O)[CH](O)[CH]3O
CACTVS 3.385Nc1ncnc2n(cnc12)[C@@H]3O[C@H](C[NH+](CC[NH3+])CC[C@H]([NH3+])C(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 2.0.6c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)C[NH+](CC[C@@H](C(=O)O)[NH3+])CC[NH3+])O)O)N
OpenEye OEToolkits 2.0.6c1nc(c2c(n1)n(cn2)C3C(C(C(O3)C[NH+](CCC(C(=O)O)[NH3+])CC[NH3+])O)O)N
FormulaC16 H29 N8 O5
Name[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl-(2-azaniumylethyl)-[(3~{S})-3-azaniumyl-4-oxidanyl-4-oxidanylidene-butyl]azanium
ChEMBL
DrugBank
ZINC
PDB chain5ntc Chain C Residue 506 [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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PDB5ntc Crystal structure of mouse CARM1 in complex with inhibitor SA0678
Resolution2.25 Å
Binding residue
(original residue number in PDB)		Y150 F151 Y154 M163 R169 G193 C194 I198 E215 A216 K242 V243 E244 E258 M269 S272
Binding residue
(residue number reindexed from 1)		Y4 F5 Y8 M17 R23 G47 C48 I52 E69 A70 K96 V97 E98 E112 M123 S126
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) D166 E258 E267 H415
Catalytic site (residue number reindexed from 1) D20 E112 E121 H269
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:5ntc, PDBe:5ntc, PDBj:5ntc
PDBsum5ntc
PubMed
UniProtQ9WVG6|CARM1_MOUSE Histone-arginine methyltransferase CARM1 (Gene Name=Carm1)

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