Structure of PDB 4jlg Chain A Binding Site BS02

Receptor Information
>4jlg Chain A (length=247) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GVCWIYYPDGGSLVGEVNEDGEMTGEKIAYVYPDERTALYGKFIDGEMIE
GKLATLMSTEEGRPHFELMPGNSVYHFDKSTSSCISTNALLPDPYESERV
YVAESLISSAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGNT
LSLDEETVIDVPEPYNHVSKYCASLGHKANHSFTPNCIYDMFVHPRFGPI
KCIRTLRAVEADEELTVAYGYDHSPPGKSGPEAPEWYQVELKAFQAT
Ligand information
Ligand ID1L8
InChIInChI=1S/C23H25F4N3O3S/c24-20-13-18(12-16-6-7-28-14-19(16)20)34(32,33)29-21(22(31)30-8-1-2-9-30)11-15-4-3-5-17(10-15)23(25,26)27/h3-5,10,12-13,21,28-29H,1-2,6-9,11,14H2/t21-/m1/s1
InChIKeyJCKGSPAAPQRPBW-OAQYLSRUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6c1cc(cc(c1)C(F)(F)F)C[C@H](C(=O)N2CCCC2)NS(=O)(=O)c3cc4c(c(c3)F)CNCC4
OpenEye OEToolkits 1.7.6c1cc(cc(c1)C(F)(F)F)CC(C(=O)N2CCCC2)NS(=O)(=O)c3cc4c(c(c3)F)CNCC4
CACTVS 3.370Fc1cc(cc2CCNCc12)[S](=O)(=O)N[CH](Cc3cccc(c3)C(F)(F)F)C(=O)N4CCCC4
CACTVS 3.370Fc1cc(cc2CCNCc12)[S](=O)(=O)N[C@H](Cc3cccc(c3)C(F)(F)F)C(=O)N4CCCC4
ACDLabs 12.01O=C(N1CCCC1)C(NS(=O)(=O)c2cc3c(c(F)c2)CNCC3)Cc4cccc(c4)C(F)(F)F
FormulaC23 H25 F4 N3 O3 S
Name8-fluoro-N-{(2R)-1-oxo-1-(pyrrolidin-1-yl)-3-[3-(trifluoromethyl)phenyl]propan-2-yl}-1,2,3,4-tetrahydroisoquinoline-6-sulfonamide
ChEMBLCHEMBL3414622
DrugBank
ZINCZINC000095920703
PDB chain4jlg Chain A Residue 402 [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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PDB4jlg (R)-PFI-2 is a potent and selective inhibitor of SETD7 methyltransferase activity in cells.
Resolution1.896 Å
Binding residue
(original residue number in PDB)		H252 V255 D256 T266 L267 S268 Y305 Y335 G336 Y337 H339 S340
Binding residue
(residue number reindexed from 1)		H136 V139 D140 T150 L151 S152 Y189 Y219 G220 Y221 H223 S224
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=8.70,IC50=2.0nM
BindingDB: IC50=2.0nM,Ki=0.330000nM
Enzymatic activity
Catalytic site (original residue number in PDB) Y245 H293 H297 Y305 Y335
Catalytic site (residue number reindexed from 1) Y129 H177 H181 Y189 Y219
Enzyme Commision number 2.1.1.364: [histone H3]-lysine(4) N-methyltransferase.
Gene Ontology
Molecular Function
GO:0016279 protein-lysine N-methyltransferase activity
GO:0140945 histone H3K4 monomethyltransferase activity
Biological Process
GO:0006355 regulation of DNA-templated transcription
Cellular Component
GO:0005694 chromosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4jlg, PDBe:4jlg, PDBj:4jlg
PDBsum4jlg
PubMed25136132
UniProtQ8WTS6|SETD7_HUMAN Histone-lysine N-methyltransferase SETD7 (Gene Name=SETD7)

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