7SGG
Crystal Structure of Danio rerio Histone Deacetylase 10 in Complex with SAHA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016236 | biological_process | macroautophagy |
A | 0016787 | molecular_function | hydrolase activity |
A | 0019213 | molecular_function | deacetylase activity |
A | 0033558 | molecular_function | protein lysine deacetylase activity |
A | 0035825 | biological_process | homologous recombination |
A | 0036269 | biological_process | swimming behavior |
A | 0046872 | molecular_function | metal ion binding |
A | 0047609 | molecular_function | acetylputrescine deacetylase activity |
A | 0047611 | molecular_function | acetylspermidine deacetylase activity |
A | 0106047 | biological_process | polyamine deacetylation |
A | 0106048 | biological_process | spermidine deacetylation |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | Motif: {"description":"Substrate specificity","evidences":[{"source":"PubMed","id":"28516954","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"28516954","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5TD7","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"28516954","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5TD7","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Site: {"description":"Substrate specificity","evidences":[{"source":"PubMed","id":"28516954","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |