Structure of PDB 5v3h Chain A Binding Site BS05

Receptor Information
>5v3h Chain A (length=438) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KDDDDKMRAEGLGGLERFCSPGKGRGLRALQPFQVGDLLFSCPAYAYVLT
VNERGNHCEYCFTRKEGLSKCGRCKQAFYCNVECQKEDWPMHKLECSPMV
VFGENWNPSETVRLTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNE
KKDLIQSDIAALHHFYSKHLGFPDNDSLVVLFAQVNCNGFTIEDEELSHL
GSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSYIDLL
YPTEDRNDRLRDSYFFTCECQECTTKDKDKAKVEIRKLSDPPKAEAIRDM
VRYARNVIEEFRRAKHYKSPSELLEICELSQEKMSSVFEDSNVYMLHMMY
QAMGVCLYMQDWEGALQYGQKIIKPYSKHYPLYSLNVASMWLKLGRLYMG
LEHKAAGEKALKKAIAIMEVAHGKDHPYISEIKQEIES
Ligand information
Ligand ID8WG
InChIInChI=1S/C20H22ClN7O/c21-16-3-1-14(2-4-16)9-27-10-15(7-22-27)8-26-11-17(12-26)23-20(29)19-13-28(25-24-19)18-5-6-18/h1-4,7,10,13,17-18H,5-6,8-9,11-12H2,(H,23,29)
InChIKeyMOWCUCXGYVJUHU-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.385Clc1ccc(Cn2cc(CN3CC(C3)NC(=O)c4cn(nn4)C5CC5)cn2)cc1
OpenEye OEToolkits 2.0.6c1cc(ccc1Cn2cc(cn2)CN3CC(C3)NC(=O)c4cn(nn4)C5CC5)Cl
ACDLabs 12.01c1(Cl)ccc(cc1)Cn5cc(CN4CC(NC(c2nnn(c2)C3CC3)=O)C4)cn5
FormulaC20 H22 Cl N7 O
NameN-[1-({1-[(4-chlorophenyl)methyl]-1H-pyrazol-4-yl}methyl)azetidin-3-yl]-1-cyclopropyl-1H-1,2,3-triazole-4-carboxamide
ChEMBLCHEMBL5187983
DrugBank
ZINC
PDB chain5v3h Chain A Residue 505 [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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PDB5v3h Small molecule inhibitors and CRISPR/Cas9 mutagenesis demonstrate that SMYD2 and SMYD3 activity are dispensable for autonomous cancer cell proliferation.
Resolution2.69 Å
Binding residue
(original residue number in PDB)		F184 T185 E187 D188 E189 Y240 Y258 L379 M412 H416
Binding residue
(residue number reindexed from 1)		F190 T191 E193 D194 E195 Y246 Y264 L385 M418 H422
Annotation score1
Binding affinityBindingDB: IC50=3.90nM
Enzymatic activity
Enzyme Commision number 2.1.1.-
2.1.1.354: [histone H3]-lysine(4) N-trimethyltransferase.
Gene Ontology
Molecular Function
GO:0000993 RNA polymerase II complex binding
GO:0002039 p53 binding
GO:0005515 protein binding
GO:0008168 methyltransferase activity
GO:0016278 lysine N-methyltransferase activity
GO:0016279 protein-lysine N-methyltransferase activity
GO:0042054 histone methyltransferase activity
GO:0046872 metal ion binding
GO:0046975 histone H3K36 methyltransferase activity
GO:0140938 histone H3 methyltransferase activity
GO:0140999 histone H3K4 trimethyltransferase activity
Biological Process
GO:0000122 negative regulation of transcription by RNA polymerase II
GO:0006325 chromatin organization
GO:0006338 chromatin remodeling
GO:0007507 heart development
GO:0008285 negative regulation of cell population proliferation
GO:0018026 peptidyl-lysine monomethylation
GO:0018027 peptidyl-lysine dimethylation
GO:0032259 methylation
GO:0043516 regulation of DNA damage response, signal transduction by p53 class mediator
GO:1901796 regulation of signal transduction by p53 class mediator
Cellular Component
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5v3h, PDBe:5v3h, PDBj:5v3h
PDBsum5v3h
PubMed29856759
UniProtQ9NRG4|SMYD2_HUMAN N-lysine methyltransferase SMYD2 (Gene Name=SMYD2)

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