1Q14
Structure and autoregulation of the yeast Hst2 homolog of Sir2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000183 | biological_process | rDNA heterochromatin formation |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016740 | molecular_function | transferase activity |
| A | 0017136 | molecular_function | histone deacetylase activity, NAD-dependent |
| A | 0031507 | biological_process | heterochromatin formation |
| A | 0034979 | molecular_function | NAD-dependent protein lysine deacetylase activity |
| A | 0045950 | biological_process | negative regulation of mitotic recombination |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046970 | molecular_function | histone H4K16 deacetylase activity, NAD-dependent |
| A | 0051287 | molecular_function | NAD binding |
| A | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 2003 |
| Chain | Residue |
| A | CYS143 |
| A | CYS146 |
| A | CYS170 |
| A | VAL172 |
| A | CYS173 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 2004 |
| Chain | Residue |
| A | LYS26 |
| A | TRP202 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00236","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20726530","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14502267","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15150415","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00236","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14502267","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14604530","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15150415","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17289592","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 240 |
| Chain | Residue | Details |
| A | ASN116 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity |
| A | ASP118 | activator, hydrogen bond acceptor |
| A | HIS135 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
