7KUR
Crystal Structure of Danio rerio Histone Deacetylase 10 Y307F Mutant in Complex with N-Acetylputrescine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
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 | 0040029 | biological_process | epigenetic regulation of gene expression |
A | 0046872 | molecular_function | metal ion binding |
A | 0047609 | molecular_function | acetylputrescine deacetylase activity |
A | 0047611 | molecular_function | acetylspermidine deacetylase activity |
A | 0090043 | biological_process | regulation of tubulin deacetylation |
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 | 1 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:28516954, ECO:0007744|PDB:5TD7 |
Chain | Residue | Details |
A | HIS137 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:28516954, ECO:0007744|PDB:5TD7 |
Chain | Residue | Details |
A | ASP22 | |
A | ALA94 | |
A | ASP174 | |
A | HIS176 | |
A | ASP267 | |
A | PHE307 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | SITE: Substrate specificity => ECO:0000269|PubMed:28516954 |
Chain | Residue | Details |
A | GLU274 |