1FY7
CRYSTAL STRUCTURE OF YEAST ESA1 HISTONE ACETYLTRANSFERASE DOMAIN COMPLEXED WITH COENZYME A
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA A 1 |
| Chain | Residue |
| A | ALA303 |
| A | COA500 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE COA A 500 |
| Chain | Residue |
| A | GLN312 |
| A | ARG313 |
| A | MET314 |
| A | GLY315 |
| A | GLY317 |
| A | LYS318 |
| A | LEU341 |
| A | SER342 |
| A | LEU344 |
| A | GLY345 |
| A | SER348 |
| A | ARG421 |
| A | HOH502 |
| A | HOH505 |
| A | HOH597 |
| A | NA1 |
| A | TRP180 |
| A | PHE258 |
| A | LEU259 |
| A | ILE305 |
| A | LEU306 |
| A | THR307 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 271 |
| Details | Domain: {"description":"MYST-type HAT","evidences":[{"source":"PROSITE-ProRule","id":"PRU01063","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 25 |
| Details | Zinc finger: {"description":"C2HC MYST-type; degenerate","evidences":[{"source":"PROSITE-ProRule","id":"PRU01063","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 21 |
| Details | Motif: {"description":"ESA1-RPD3 motif"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"12368900","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"17223684","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"18245364","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000303"},{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11106757","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12368900","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mj9 |
| Chain | Residue | Details |
| A | GLU338 | |
| A | CYS304 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 525 |
| Chain | Residue | Details |
| A | CYS304 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | GLU338 | activator, proton acceptor, proton donor |
