Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000118 | cellular_component | histone deacetylase complex |
| A | 0004407 | molecular_function | histone deacetylase activity |
| A | 0006325 | biological_process | chromatin organization |
| A | 0016575 | biological_process | histone deacetylation |
| B | 0000118 | cellular_component | histone deacetylase complex |
| B | 0004407 | molecular_function | histone deacetylase activity |
| B | 0006325 | biological_process | chromatin organization |
| B | 0016575 | biological_process | histone deacetylation |
| C | 0000118 | cellular_component | histone deacetylase complex |
| C | 0004407 | molecular_function | histone deacetylase activity |
| C | 0006325 | biological_process | chromatin organization |
| C | 0016575 | biological_process | histone deacetylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | HOH289 |
| A | ASP707 |
| A | HIS709 |
| A | ASP801 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 402 |
| Chain | Residue |
| A | CYS533 |
| A | CYS535 |
| A | HIS541 |
| A | CYS618 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 904 |
| Chain | Residue |
| A | ASP707 |
| A | HIS709 |
| A | SER728 |
| A | LEU729 |
| A | ASP705 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 905 |
| Chain | Residue |
| A | HOH41 |
| A | HOH52 |
| A | PHE718 |
| A | ASP721 |
| A | VAL724 |
| A | PHE755 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 403 |
| Chain | Residue |
| B | HOH142 |
| B | HOH352 |
| B | ASP707 |
| B | HIS709 |
| B | ASP801 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 404 |
| Chain | Residue |
| B | CYS533 |
| B | CYS535 |
| B | HIS541 |
| B | CYS618 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K B 904 |
| Chain | Residue |
| B | ASP705 |
| B | ASP707 |
| B | HIS709 |
| B | SER728 |
| B | LEU729 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 905 |
| Chain | Residue |
| B | HOH17 |
| B | HOH34 |
| B | PHE718 |
| B | ASP721 |
| B | VAL724 |
| B | PHE755 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 405 |
| Chain | Residue |
| C | HOH291 |
| C | ASP707 |
| C | HIS709 |
| C | ASP801 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 406 |
| Chain | Residue |
| C | CYS533 |
| C | CYS535 |
| C | HIS541 |
| C | CYS618 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K C 904 |
| Chain | Residue |
| C | ASP705 |
| C | ASP707 |
| C | HIS709 |
| C | SER728 |
| C | LEU729 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K C 905 |
| Chain | Residue |
| C | HOH45 |
| C | HOH190 |
| C | PHE718 |
| C | ASP721 |
| C | VAL724 |
| C | PHE755 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"Q8C2B3","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18285338","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Site: {"description":"Contributes to catalysis","evidences":[{"source":"PubMed","id":"18285338","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
