Structure of PDB 5fwa Chain A Binding Site BS01

Receptor Information
>5fwa Chain A (length=339) Species: 10090 (Mus musculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DTWQDEEYFDSYGTLKLHLEMLADQPRTTKYHSVILQNKESLKDKVILDV
GCGTGIISLFCAHHARPKAVYAVEASDMAQHTSQLVLQNGFADTITVFQQ
KVEDVVLPEKVDVLVSEWMGTCLLFEFMIESILYARDTWLKGDGIIWPTT
AALHLVPCSAEKDYHSKVLFWDNAYEFNLSALKSLAIKEFFSRPKSNHIL
KPEDCLSEPCTILQLDMRTVQVPDLETMRGELRFDIQKAGTLHGFTAWFS
VYFQSLEEGQPQQVLSTGPLHPTTHWKQTLFMMDDPVPVHTGDVVTGSVV
LQRNPVWRRHMSVSLSWVVTSALDPTSQRVGEKVFPIWW
Ligand information
Ligand IDJ7C
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)/t5-,7-,8-,11-/m1/s1
InChIKeyOIGRVZYOOMUALG-IOSLPCCCSA-N
SMILES
SoftwareSMILES
CACTVS 3.385NC(=N)NCC[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.7.6[H]/N=C(\N)/NCC[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)O)O
CACTVS 3.385NC(=N)NCC[CH]1O[CH]([CH](O)[CH]1O)n2cnc3c(N)ncnc23
ACDLabs 12.01n1c(c2c(nc1)n(cn2)C3C(C(O)C(CCN/C(N)=N)O3)O)N
OpenEye OEToolkits 1.7.6c1nc(c2c(n1)n(cn2)C3C(C(C(O3)CCNC(=N)N)O)O)N
FormulaC12 H18 N8 O3
Name9-(6-carbamimidamido-5,6-dideoxy-beta-D-ribo-hexofuranosyl)-9H-purin-6-amine
ChEMBL
DrugBank
ZINCZINC000584905108
PDB chain5fwa Chain A Residue 1446 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5fwa Structural studies of protein arginine methyltransferase 2 reveal its interactions with potential substrates and inhibitors.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		Y114 F115 Y118 G157 E180 A181 K207 E223 W224 M225 E232 M234 S237
Binding residue
(residue number reindexed from 1)		Y8 F9 Y12 G51 E74 A75 K101 E117 W118 M119 E126 M128 S131
Annotation score1
Binding affinityMOAD: ic50=16.3uM
PDBbind-CN: -logKd/Ki=4.79,IC50=16.3uM
Enzymatic activity
Catalytic site (original residue number in PDB) D130 E223 E232 H381
Catalytic site (residue number reindexed from 1) D24 E117 E126 H275
Enzyme Commision number 2.1.1.125: Transferred entry: 2.1.1.319, 2.1.1.320, 2.1.1.321 and 2.1.1.322.
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
GO:0016274 protein-arginine N-methyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0018216 peptidyl-arginine methylation
GO:0032259 methylation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5fwa, PDBe:5fwa, PDBj:5fwa
PDBsum5fwa
PubMed27879050
UniProtQ3UKX1

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