Structure of PDB 5wcg Chain A Binding Site BS04

Receptor Information
>5wcg Chain A (length=430) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RAELGGLERFCSPGKGRGLRALQPFQVGDLLFSCPAYAYVLTVNERGNHC
EYCFTRKEGLSKCGRCKQAFYCNVECQKEDWPMHKLECSPMVVFGENWNP
SETVRLTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNEKKDLIQSD
IAALHHFYSKHLEFPDNDSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDV
ALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSYIDLLYPTEDRND
RLRDSYFFTCECQECTTKDKDKAKVEIRKLSDPPKAEAIRDMVRYARNVI
EEFRRAKHYKSPSELLEICELSQEKMSSVFEDSNVYMLHMMYQAMGVCLY
MQDWEGALQYGQKIIKPYSKHYPLYSLNVASMWLKLGRLYMGLEHKAAGE
KALKKAIAIMEVAHGKDHPYISEIKQEIES
Ligand information
Ligand IDA4M
InChIInChI=1S/C26H38N10O/c1-18-29-24(27)23-25(30-18)36(17-28-23)21-15-35(16-21)26(37)22-13-20(32(2)31-22)14-33-9-11-34(12-10-33)19-7-5-3-4-6-8-19/h13,17,19,21H,3-12,14-16H2,1-2H3,(H2,27,29,30)
InChIKeyYBGLVGMKTGYRQH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.6Cc1nc(c2c(n1)n(cn2)C3CN(C3)C(=O)c4cc(n(n4)C)CN5CCN(CC5)C6CCCCCC6)N
ACDLabs 12.01c21c(nc(nc1n(cn2)C6CN(C(c5cc(CN4CCN(C3CCCCCC3)CC4)n(C)n5)=O)C6)C)N
CACTVS 3.385Cn1nc(cc1CN2CCN(CC2)C3CCCCCC3)C(=O)N4CC(C4)n5cnc6c(N)nc(C)nc56
FormulaC26 H38 N10 O
Name[3-(6-amino-2-methyl-9H-purin-9-yl)azetidin-1-yl]{5-[(4-cycloheptylpiperazin-1-yl)methyl]-1-methyl-1H-pyrazol-3-yl}methanone
ChEMBLCHEMBL4439045
DrugBank
ZINC
PDB chain5wcg Chain A Residue 504 [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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PDB5wcg The crystal structure of SMYD2 in complex with compound MTF003
Resolution2.02 Å
Binding residue
(original residue number in PDB)		K17 H137 C181 N182 G183 F184 A203 N206 H207 Y240 Y258 F260
Binding residue
(residue number reindexed from 1)		K15 H135 C179 N180 G181 F182 A201 N204 H205 Y238 Y256 F258
Annotation score1
Binding affinityBindingDB: IC50=7000nM
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:5wcg, PDBe:5wcg, PDBj:5wcg
PDBsum5wcg
PubMed
UniProtQ9NRG4|SMYD2_HUMAN N-lysine methyltransferase SMYD2 (Gene Name=SMYD2)

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