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 | NAD-dependent histone deacetylase activity |
| 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 | NAD-dependent histone H4K16 deacetylase activity |
| 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 | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:20726530 |
| Chain | Residue | Details |
| A | HIS135 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415 |
| Chain | Residue | Details |
| A | GLY32 | |
| A | GLN115 | |
| A | GLY223 | |
| A | ASN248 | |
| A | SER270 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:14604530, ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592 |
| Chain | Residue | Details |
| A | CYS143 | |
| A | CYS146 | |
| A | CYS170 | |
| A | CYS173 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylserine => ECO:0007744|PubMed:22814378 |
| Chain | Residue | Details |
| A | SER2 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956 |
| Chain | Residue | Details |
| A | SER340 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 240 |
| Chain | Residue | Details |
| A | PRO42 | hydrogen bond acceptor, steric role |
| A | ASP43 | hydrogen bond acceptor, hydrogen bond donor, steric role |
| A | PHE44 | steric role, van der waals interaction |
| A | ARG45 | electrostatic stabiliser, hydrogen bond donor |
| 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 |
