6VNQ
Crystal Structure of Danio rerio Histone Deacetylase 10 in Complex with Bishydroxamic Acid Based Inhibitor
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 PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | binding site for residue R5G A 701 |
| Chain | Residue |
| A | GLU24 |
| A | TRP205 |
| A | ASP267 |
| A | GLU274 |
| A | GLY305 |
| A | TYR307 |
| A | ZN704 |
| A | HOH801 |
| A | HOH996 |
| A | ASN93 |
| A | ALA94 |
| A | HIS136 |
| A | HIS137 |
| A | GLY145 |
| A | PHE146 |
| A | ASP174 |
| A | HIS176 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 702 |
| Chain | Residue |
| A | LYS75 |
| A | HIS201 |
| A | PO4708 |
| A | HOH809 |
| A | HOH945 |
| A | HOH982 |
| A | HOH983 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 703 |
| Chain | Residue |
| A | VAL35 |
| A | GLU38 |
| A | ALA39 |
| A | HOH985 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 704 |
| Chain | Residue |
| A | ASP174 |
| A | HIS176 |
| A | ASP267 |
| A | R5G701 |
| A | HOH801 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue K A 705 |
| Chain | Residue |
| A | ASP172 |
| A | ASP174 |
| A | HIS176 |
| A | SER195 |
| A | TRP196 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue K A 706 |
| Chain | Residue |
| A | PHE185 |
| A | ASP188 |
| A | VAL191 |
| A | PHE224 |
| A | HOH860 |
| A | HOH977 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | binding site for residue PO4 A 707 |
| Chain | Residue |
| A | GLN56 |
| A | LYS106 |
| A | HIS201 |
| A | ASP212 |
| A | TYR213 |
| A | ASN231 |
| A | HOH818 |
| A | HOH827 |
| A | HOH838 |
| A | HOH950 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue PO4 A 708 |
| Chain | Residue |
| A | LYS75 |
| A | HIS201 |
| A | ASN231 |
| A | LYS232 |
| A | SER340 |
| A | GLU343 |
| A | EDO702 |
| A | HOH816 |
| A | HOH917 |
| A | HOH953 |
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 |
