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7SGI

Crystal Structure of Danio rerio Histone Deacetylase 10 in Complex with Inhibitor 14

Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0008270molecular_functionzinc ion binding
A0016236biological_processmacroautophagy
A0016787molecular_functionhydrolase activity
A0019213molecular_functiondeacetylase activity
A0033558molecular_functionprotein lysine deacetylase activity
A0035825biological_processhomologous recombination
A0036269biological_processswimming behavior
A0040029biological_processepigenetic regulation of gene expression
A0046872molecular_functionmetal ion binding
A0047609molecular_functionacetylputrescine deacetylase activity
A0047611molecular_functionacetylspermidine deacetylase activity
A0090043biological_processregulation of tubulin deacetylation
A0106047biological_processpolyamine deacetylation
A0106048biological_processspermidine deacetylation
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:28516954, ECO:0007744|PDB:5TD7
ChainResidueDetails
AHIS137

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:28516954, ECO:0007744|PDB:5TD7
ChainResidueDetails
AASP22
AALA94
AASP174
AHIS176
AASP267
ATYR307

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Substrate specificity => ECO:0000269|PubMed:28516954
ChainResidueDetails
AGLU274

219869

PDB entries from 2024-05-15

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