5IKK
Structure of the histone deacetylase Clr3
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000118 | cellular_component | histone deacetylase complex |
| A | 0000183 | biological_process | rDNA heterochromatin formation |
| A | 0000775 | cellular_component | chromosome, centromeric region |
| A | 0000781 | cellular_component | chromosome, telomeric region |
| A | 0000785 | cellular_component | chromatin |
| A | 0000791 | cellular_component | euchromatin |
| A | 0004407 | molecular_function | histone deacetylase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005721 | cellular_component | pericentric heterochromatin |
| A | 0005730 | cellular_component | nucleolus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006325 | biological_process | chromatin organization |
| A | 0006338 | biological_process | chromatin remodeling |
| A | 0010468 | biological_process | regulation of gene expression |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0030466 | biological_process | silent mating-type cassette heterochromatin formation |
| A | 0031078 | molecular_function | histone H3K14 deacetylase activity, hydrolytic mechanism |
| A | 0031507 | biological_process | heterochromatin formation |
| A | 0031508 | biological_process | pericentric heterochromatin formation |
| A | 0031509 | biological_process | subtelomeric heterochromatin formation |
| A | 0031934 | cellular_component | mating-type region heterochromatin |
| A | 0033553 | cellular_component | rDNA heterochromatin |
| A | 0040029 | biological_process | epigenetic regulation of gene expression |
| A | 0070824 | cellular_component | SHREC complex |
| A | 0140720 | cellular_component | subtelomeric heterochromatin |
| A | 0141221 | molecular_function | histone deacetylase activity, hydrolytic mechanism |
| A | 1902794 | biological_process | siRNA-independent facultative heterochromatin formation |
| A | 1990342 | cellular_component | heterochromatin island |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 701 |
| Chain | Residue |
| A | HIS195 |
| A | ASP234 |
| A | HIS236 |
| A | ASP327 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue K A 702 |
| Chain | Residue |
| A | HOH856 |
| A | PHE245 |
| A | ASP248 |
| A | VAL251 |
| A | ARG284 |
| A | HOH822 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue ZN A 703 |
| Chain | Residue |
| A | HIS68 |
| A | HIS77 |
| A | CYS162 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue K A 704 |
| Chain | Residue |
| A | ASP232 |
| A | ASP234 |
| A | HIS236 |
| A | SER255 |
| A | LEU256 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue NO3 A 705 |
| Chain | Residue |
| A | ARG64 |
| A | MET65 |
| A | ARG66 |
| A | LYS452 |
| A | ASN476 |
| A | HOH808 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue NO3 A 706 |
| Chain | Residue |
| A | TYR313 |
| A | ASP316 |
| A | HIS346 |
| A | ARG390 |
| A | LEU391 |
| A | HOH967 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue NO3 A 707 |
| Chain | Residue |
| A | SER412 |
| A | GLN413 |
| A | TYR414 |
| A | ARG419 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 708 |
| Chain | Residue |
| A | TYR302 |
| A | ARG416 |
| A | ARG419 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 709 |
| Chain | Residue |
| A | ARG440 |
| A | HIS488 |
| A | ASP513 |
| A | VAL515 |
| A | SER516 |
| A | ASP531 |
| A | HOH925 |
| A | HOH954 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 710 |
| Chain | Residue |
| A | ASP80 |
| A | GLY366 |
| A | TYR367 |
| A | LEU369 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 711 |
| Chain | Residue |
| A | TYR129 |
| A | GLU617 |
| A | PRO621 |
| A | LYS646 |
| A | ARG647 |
| A | ARG648 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 712 |
| Chain | Residue |
| A | PRO427 |
| A | ASP429 |
| A | VAL432 |
| A | HOH906 |
| A | HOH934 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
