2HJH
Crystal Structure of the Sir2 deacetylase
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 800 |
| Chain | Residue |
| A | CYS372 |
| A | CYS375 |
| A | CYS396 |
| A | CYS399 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 800 |
| Chain | Residue |
| B | CYS372 |
| B | CYS375 |
| B | CYS396 |
| B | CYS399 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE XYQ A 1222 |
| Chain | Residue |
| A | GLY262 |
| A | ALA263 |
| A | GLY264 |
| A | THR267 |
| A | ASP273 |
| A | PHE274 |
| A | ARG275 |
| A | GLN344 |
| A | HIS364 |
| A | GLY471 |
| A | THR472 |
| A | SER473 |
| A | ASN496 |
| A | ARG497 |
| A | ASP498 |
| A | GLY511 |
| A | TYR512 |
| A | CYS513 |
| A | HOH1238 |
| A | HOH1243 |
| A | HOH1247 |
| A | HOH1275 |
| A | HOH1319 |
| A | HOH1322 |
| A | HOH1479 |
| A | LYS222 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE XYQ B 1222 |
| Chain | Residue |
| B | LYS222 |
| B | GLY262 |
| B | ALA263 |
| B | GLY264 |
| B | THR267 |
| B | ASP273 |
| B | PHE274 |
| B | ARG275 |
| B | GLN344 |
| B | HIS364 |
| B | GLY471 |
| B | THR472 |
| B | SER473 |
| B | ASN496 |
| B | ARG497 |
| B | ASP498 |
| B | GLY511 |
| B | TYR512 |
| B | CYS513 |
| B | HOH1246 |
| B | HOH1255 |
| B | HOH1256 |
| B | HOH1257 |
| B | HOH1268 |
| B | HOH1296 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NCA A 900 |
| Chain | Residue |
| A | ILE271 |
| A | PRO272 |
| A | PHE274 |
| A | PHE280 |
| A | ILE346 |
| A | HOH1482 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NCA B 901 |
| Chain | Residue |
| B | ILE271 |
| B | PRO272 |
| B | ASP273 |
| B | PHE274 |
| B | PHE280 |
| B | HOH1289 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00236","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 42 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23307867","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2006","submissionDatabase":"PDB data bank","title":"Autoregulation of the yeast Sir2 deacetylase by reaction and trapping of a pseudosubstrate motif in the active site.","authors":["Hall B.E.","Buchberger J.R.","Gerber S.A.","Ambrosio A.L.B.","Gygi S.P.","Filman D.","Moazed D.","Ellenberger T."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P53686","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23307867","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
