2VQJ,1C3R,3MAX


Conserved Protein Domain Family
HDAC

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cd09301: HDAC 
Click on image for an interactive view with Cn3D
Histone deacetylase (HDAC) classes I, II, IV and related proteins
The HDAC/HDAC-like family includes Zn-dependent histone deacetylase classes I, II and IV (class III HDACs, also called sirtuins, are NAD-dependent and structurally unrelated, and therefore not part of this family). Histone deacetylases catalyze hydrolysis of N(6)-acetyl-lysine residues in histone amino termini to yield a deacetylated histone (EC 3.5.1.98), as opposed to the acetylation reaction by some histone acetyltransferases (EC 2.3.1.48). Deacetylases of this family are involved in signal transduction through histone and other protein modification, and can repress/activate transcription of a number of different genes. They usually act via the formation of large multiprotein complexes. They are involved in various cellular processes, including cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and post-translational control of the acetyl coenzyme A synthetase. In mammals, they are known to be involved in progression of different tumors. Specific inhibitors of mammalian histone deacetylases are an emerging class of promising novel anticancer drugs.
Statistics
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PSSM-Id: 212512
Aligned: 8 rows
Threshold Bit Score: 291.646
Created: 18-Nov-2009
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
active siteZn binding site
Conserved site includes 9 residues -Click on image for an interactive view with Cn3D
Feature 1:active site [active site]
Evidence:
  • Comment:Active site includes Zn binding site, lipophilic tube and foot pocket.
  • Structure:3MAX: human histone deacetylase 2 binds amino benzamide (inhibitor) and Zn ion; contacts at 4A.
  • Structure:2VQJ: human histone deacetylase 4 binds trifluoromethylketone inhbitor and Zn ion; contacts at 4A.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                                                     
2VQJ_A     37 RIQSIWSRlqetglrgkcecirgrkatleelqtvHSEAHTLLYgtnplnrqkldskkllgslasvfvrlpcggvgvdsdt 116 human
1C3R_A     27 RVSLLLRFkdamnlidekeliksrpatkeelllfHTEDYINTLmeaersqsvpkgarek--------------yniggye 92  Aquifex aeolicus
Q96DB2     41 KWGKVINFlkeekllsdsmlveareaseedllvvHTRRYLNELkwsfavatiteipp-----------------viflpn 103 human
3MAX_A     28 RIRMTHNLllnyglyrkmeiyrphkataeemtkyHSDEYIKFLrsirpdnmseyskqmq--------------rfnvged 93  human
AEB09430   23 RLRDFPEAleellqrpeislfecpraskelilkvHAPEMLQGVard---------------------------------- 68  Desulfobacca aceto...
ADC66595   23 RLKDFPEAfeelksfenfkliecpevseelilkvHDPELLEGVkad---------------------------------- 68  Ferroglobus placid...
ADI01978   29 AMTDLIEAgkiglftpait-----qeteellnqcHSARHIAMVkae---------------------------------- 69  Syntrophothermus l...
ADC66358   25 GFESLIEEfkklgaavfep----eevdenlllkvHTEKFLEEQskn---------------------------------- 66  Ferroglobus placid...
Feature 1                                                ##       ##                          
2VQJ_A    117 iwnevhsaGAARLAVGCVVELVFKVatgelknGFAVVr--PPGHHAeestpMGFCYFNSVAVAAKLlqqrl-svskILIV 193 human
1C3R_A     93 npvsyamfTGSSLATGSTVQAIEEFlkg--nvAFNPA---GGMHHAfksraNGFCYINNPAVGIEYlrkk--gfkrILYI 165 Aquifex aeolicus
Q96DB2    104 flvqrkvlRPLRTQTGGTIMAGKLAve----rGWAINv-gGGFHHCssdrgGGFCAYADITLAIKFlfervegisrATII 178 human
3MAX_A     94 cpvfdglfEFCQLSTGGSVAGAVKLnrqqtdmAVNWA---GGLHHAkkseaSGFCYVNDIVLAILEllky---hqrVLYI 167 human
AEB09430   69 -----rmcSTAYESVGGVVAAMEALakgeldrAFCFIg--AGGHHAgyrsfWGACCFNDVVIALTQvrevt-slrrFAIV 140 Desulfobacca aceto...
ADC66595   69 -----plcSTAWHSAGGVVKATEMVyegelrnAFCYIg--AGGHHSgkrifWGYCCFNDVILAMRNlrdky-gdvkFAIV 140 Ferroglobus placid...
ADI01978   70 -----hyhDVALLSAAGVVEAAERLatgdlefAFCFVg--AAGHHAgydrfWGFCYYNDAVMAIKKlral--gikrVMII 140 Syntrophothermus l...
ADC66358   67 -----wyyRGAKLTVGGVVKACELVwk---ekGNAVVfsvAAGHHAgrnhaWGGTYLNCAGTALVRlrel--glrrIALI 136 Ferroglobus placid...
Feature 1       # #                                                                           
2VQJ_A    194 DWDVHHGNGTQQAFYsdpsvLYMSLHryddgnffpgsgapdevgtgpgvGFNVNMAFtggldppmgDAEYLAAFRTVvmp 273 human
1C3R_A    166 DLDAHHCDGVQEAFYdtdqvFVLSLHqspeyafpfekgfleeigegkgkGYNLNIPLpkg----lnDNEFLFALEKSlei 241 Aquifex aeolicus
Q96DB2    179 DLDAHQGNGHERDFMddkrvYIMDVYnrhiypg----------drfakqAIRRKVELewg----teDDEYLDKVERNikk 244 human
3MAX_A    168 DIDIHHGDGVEEAFYttdrvMTVSFHkygeyfpgtgd--lrdigagkgkYYAVNFPMrdg----idDESYGQIFKPIisk 241 human
AEB09430  141 DTDAHHGDGTRQLVQhdpevLHLCFCdedy---------------rsedGTKIDVDVyqyswrqdpDQEYLAAVQSHipl 205 Desulfobacca aceto...
ADC66595  141 DTDAHHGDGTRELVKdddkvLHYCICasdy---------------espdGLKIDRSYig-----lsRKEYVDLVREFadr 200 Ferroglobus placid...
ADI01978  141 DVDPHFGDGTRDLIGadpdvIHVNFHsgswriv----------edpelnNYDIGLGSg-------gDSDFIDALNRVlsr 203 Syntrophothermus l...
ADC66358  137 DTDAHHGDGDRDVLFgdrnaLHICFCwnni---------------vedgGTKICVRVsdv----dgDEEYLERVLDTfgi 197 Ferroglobus placid...
Feature 1                     #                                           # #                
2VQJ_A    274 iasefaPDVVLVSSGFDAveghptplggyNLSARCFGYLTKQLMgla----ggrIVLALEGGHdltAICDASEACVSAL 348 human
1C3R_A    242 vkevfePEVYLLQLGTDPlledy--lskfNLSNVAFLKAFNIVRevf-----geGVYLGGGGYhpyALARAWTLIWCEL 313 Aquifex aeolicus
Q96DB2    245 slqehlPDVVVYNAGTDIlegdr--lgglSISPAGIVKRDELVFrmvrg-rrvpILMVTSGGYq-kRTARIIADSILNL 319 human
3MAX_A    242 vmemyqPSAVVLQCGADSlsgdr--lgcfNLTVKGHAKCVEVVKtfn-----lpLLMLGGGGYtirNVARCWTYETAVA 313 human
AEB09430  206 v-ldfkPELLVWYYGFDThkyd---ygsiGLTEKAFFQICQVMLdtae--alkiPLQVVLGGG---SLAELATATIPGI 275 Desulfobacca acetox...
ADC66595  201 a-ekfsPDLIFWYFGHDThvgd---ygdiGLTVNEYVEIAKIVKesakkicdekLVVVLGGGSvpyIAKISTLSIIKEL 275 Ferroglobus placidu...
ADI01978  204 ---swdYEILMIIFGHDShild---yggfALTEISFKHLAEAIKefaa---gkpVLFILSGGAnpeVAKTVIPMVIKTF 273 Syntrophothermus li...
ADC66358  198 i-ekfePEMILHFFGHDThkyd---ygslGLSEEFFPKLAKEIKnladeicegrYVLIDGGGAnreVGMKIWREIVKIL 272 Ferroglobus placidu...

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