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7SGG

Crystal Structure of Danio rerio Histone Deacetylase 10 in Complex with SAHA

Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008270molecular_functionzinc ion binding
A0016236biological_processmacroautophagy
A0016787molecular_functionhydrolase activity
A0019213molecular_functiondeacetylase activity
A0033558molecular_functionprotein lysine deacetylase activity
A0035825biological_processhomologous recombination
A0036269biological_processswimming behavior
A0046872molecular_functionmetal ion binding
A0047609molecular_functionacetylputrescine deacetylase activity
A0047611molecular_functionacetylspermidine deacetylase activity
A0106047biological_processpolyamine deacetylation
A0106048biological_processspermidine deacetylation
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsMotif: {"description":"Substrate specificity","evidences":[{"source":"PubMed","id":"28516954","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"28516954","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5TD7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28516954","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5TD7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Substrate specificity","evidences":[{"source":"PubMed","id":"28516954","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2025-07-16

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