1Q1A
Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP ribose and histone peptide
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 701 |
| Chain | Residue |
| A | CYS143 |
| A | CYS146 |
| A | CYS170 |
| A | CYS173 |
| site_id | AC2 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE OAD A 1001 |
| Chain | Residue |
| A | PHE44 |
| A | ARG45 |
| A | TYR52 |
| A | PRO61 |
| A | GLN115 |
| A | HIS135 |
| A | ILE181 |
| A | VAL182 |
| A | PHE184 |
| A | GLY223 |
| A | THR224 |
| A | SER225 |
| A | VAL228 |
| A | ASN248 |
| A | LEU249 |
| A | GLN268 |
| A | TYR269 |
| A | SER270 |
| A | HOH1002 |
| A | HOH1013 |
| A | HOH1027 |
| A | HOH1124 |
| A | HOH1158 |
| A | HOH1213 |
| B | ALY353 |
| A | GLY32 |
| A | ALA33 |
| A | GLY34 |
| A | THR37 |
| A | ASP43 |
Functional Information from PROSITE/UniProt
| site_id | PS00047 |
| Number of Residues | 5 |
| Details | HISTONE_H4 Histone H4 signature. GAKRH |
| Chain | Residue | Details |
| B | GLY351-HIS355 |
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 | 28 |
| 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":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"22343720","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"11080160","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15150415","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17289592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19113941","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
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 |
