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7JVV

Crystal structure of human histone deacetylase 8 (HDAC8) E66D/Y306F double mutation complexed with a tetrapeptide substrate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000118cellular_componenthistone deacetylase complex
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000228cellular_componentnuclear chromosome
A0004407molecular_functionhistone deacetylase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0005737cellular_componentcytoplasm
A0006325biological_processchromatin organization
A0007064biological_processmitotic sister chromatid cohesion
A0016787molecular_functionhydrolase activity
A0030544molecular_functionHsp70 protein binding
A0031078molecular_functionhistone H3K14 deacetylase activity
A0031397biological_processnegative regulation of protein ubiquitination
A0031647biological_processregulation of protein stability
A0032129molecular_functionhistone H3K9 deacetylase activity
A0032204biological_processregulation of telomere maintenance
A0033558molecular_functionprotein lysine deacetylase activity
A0034739molecular_functionhistone H4K16 deacetylase activity
A0040029biological_processepigenetic regulation of gene expression
A0042903molecular_functiontubulin deacetylase activity
A0046872molecular_functionmetal ion binding
A0051879molecular_functionHsp90 protein binding
A0140297molecular_functionDNA-binding transcription factor binding
A0140937molecular_functionhistone H4K12 deacetylase activity
A0160008molecular_functionprotein decrotonylase activity
A0160009molecular_functionhistone decrotonylase activity
A0180032molecular_functionhistone H4K5 deacetylase activity
A0180033molecular_functionhistone H4K48 deacetylase activity
A1990162molecular_functionhistone H3K4 deacetylase activity
B0000118cellular_componenthistone deacetylase complex
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0000228cellular_componentnuclear chromosome
B0004407molecular_functionhistone deacetylase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005694cellular_componentchromosome
B0005737cellular_componentcytoplasm
B0006325biological_processchromatin organization
B0007064biological_processmitotic sister chromatid cohesion
B0016787molecular_functionhydrolase activity
B0030544molecular_functionHsp70 protein binding
B0031078molecular_functionhistone H3K14 deacetylase activity
B0031397biological_processnegative regulation of protein ubiquitination
B0031647biological_processregulation of protein stability
B0032129molecular_functionhistone H3K9 deacetylase activity
B0032204biological_processregulation of telomere maintenance
B0033558molecular_functionprotein lysine deacetylase activity
B0034739molecular_functionhistone H4K16 deacetylase activity
B0040029biological_processepigenetic regulation of gene expression
B0042903molecular_functiontubulin deacetylase activity
B0046872molecular_functionmetal ion binding
B0051879molecular_functionHsp90 protein binding
B0140297molecular_functionDNA-binding transcription factor binding
B0140937molecular_functionhistone H4K12 deacetylase activity
B0160008molecular_functionprotein decrotonylase activity
B0160009molecular_functionhistone decrotonylase activity
B0180032molecular_functionhistone H4K5 deacetylase activity
B0180033molecular_functionhistone H4K48 deacetylase activity
B1990162molecular_functionhistone H3K4 deacetylase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:19053282
ChainResidueDetails
AHIS143
BHIS143

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:19053282
ChainResidueDetails
AASP101
AGLY151
APHE306
BASP101
BGLY151
BPHE306

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:17721440
ChainResidueDetails
AASP178
AHIS180
AASP267
BASP178
BHIS180
BASP267

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:15242608
ChainResidueDetails
ASER39
BSER39

227344

PDB entries from 2024-11-13

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