Online Services

●I-TASSER ●I-TASSER-MTD ●C-I-TASSER ●CR-I-TASSER ●QUARK ●C-QUARK ●LOMETS ●MUSTER ●CEthreader ●SEGMER ●DeepFold ●DeepFoldRNA ●FoldDesign ●COFACTOR ●COACH ●MetaGO ●TripletGO ●IonCom ●FG-MD ●ModRefiner ●REMO ●DEMO ●DEMO-EM ●SPRING ●COTH ●Threpp ●PEPPI ●BSpred ●ANGLOR ●EDock ●BSP-SLIM ●SAXSTER ●FUpred ●ThreaDom ●ThreaDomEx ●EvoDesign ●BindProf ●BindProfX ●SSIPe ●GPCR-I-TASSER ●MAGELLAN ●ResQ ●STRUM ●DAMpred

●TM-score ●TM-align ●US-align ●MM-align ●RNA-align ●NW-align ●LS-align ●EDTSurf ●MVP ●MVP-Fit ●SPICKER ●HAAD ●PSSpred ●3DRobot ●MR-REX ●I-TASSER-MR ●SVMSEQ ●NeBcon ●ResPRE ●TripletRes ●DeepPotential ●WDL-RF ●ATPbind ●DockRMSD ●DeepMSA ●FASPR ●EM-Refiner ●GPU-I-TASSER

●BioLiP ●E. coli ●GLASS ●GPCR-HGmod ●GPCR-RD ●GPCR-EXP ●Tara-3D ●TM-fold ●DECOYS ●POTENTIAL ●RW/RWplus ●EvoEF ●HPSF ●THE-DB ●ADDRESS ●Alpaca-Antibody ●CASP7 ●CASP8 ●CASP9 ●CASP10 ●CASP11 ●CASP12 ●CASP13 ●CASP14

Structure of PDB 1w22 Chain B Binding Site BS01

Receptor Information >1w22 Chain B (length=350) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure] VPVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQMRIVKPKVASM EEMATFHTDAYLQHLQKVSQEYGLGYDCPATEGIFDYAAAIGGATITAAQ CLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILY VDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRY YSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPM CSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILG KTLSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLK

Ligand information Ligand ID NHB InChI InChI=1S/C17H15N3O4S2/c1-20(13-7-5-12(6-8-13)17(21)19-22)26(23,24)16-10-9-15(25-16)14-4-2-3-11-18-14/h2-11,22H,1H3,(H,19,21) InChIKey LFGYSFPVLMPUPE-UHFFFAOYSA-N SMILES Software SMILES CACTVS 3.341 CN(c1ccc(cc1)C(=O)NO)[S](=O)(=O)c2sc(cc2)c3ccccn3 OpenEye OEToolkits 1.5.0 CN(c1ccc(cc1)C(=O)NO)S(=O)(=O)c2ccc(s2)c3ccccn3 ACDLabs 10.04 O=S(=O)(c2sc(c1ncccc1)cc2)N(c3ccc(C(=O)NO)cc3)C Formula C17 H15 N3 O4 S2 Name N-HYDROXY-4-(METHYL{[5-(2-PYRIDINYL)-2-THIENYL]SULFONYL}AMINO)BENZAMIDE ChEMBL DrugBank DB02917 ZINC ZINC000005850198 PDB chain 1w22 Chain A Residue 1378 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure Global view Local view Structure summary [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] PDB 1w22 Crystal Structure of a Eukaryotic Zn-Dependent Histone Deacetylase,Human Hdac8,Complexed with a Hydroxamic Acid Inhibitor Resolution 2.5 Å Binding residue (original residue number in PDB) P273 Y306 Binding residue (residue number reindexed from 1) P249 Y282 Annotation score 1 Binding affinity MOAD: ic50=175.5nM

Enzymatic activity Enzyme Commision number 3.5.1.- 3.5.1.98: histone deacetylase.

Gene Ontology Molecular Function GO:0004407 histone deacetylase activity GO:0005515 protein binding GO:0016787 hydrolase activity GO:0030544 Hsp70 protein binding GO:0033558 protein lysine deacetylase activity GO:0046872 metal ion binding GO:0051879 Hsp90 protein binding GO:0140297 DNA-binding transcription factor binding GO:0160008 protein decrotonylase activity GO:0160009 histone decrotonylase activity

	Biological Process
GO:0000122	negative regulation of transcription by RNA polymerase II
GO:0006325	chromatin organization
GO:0007064	mitotic sister chromatid cohesion
GO:0031397	negative regulation of protein ubiquitination
GO:0031647	regulation of protein stability
GO:0032204	regulation of telomere maintenance
GO:0040029	epigenetic regulation of gene expression

	Cellular Component
GO:0000118	histone deacetylase complex
GO:0000228	nuclear chromosome
GO:0005634	nucleus
GO:0005654	nucleoplasm
GO:0005694	chromosome
GO:0005737	cytoplasm

View graph for Molecular Function

View graph for Biological Process

View graph for Cellular Component