3TO6
Crystal structure of yeast Esa1 HAT domain complexed with H4K16CoA bisubstrate inhibitor
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE CMC B 600 |
| Chain | Residue |
| A | HOH3 |
| A | GLN312 |
| A | ARG313 |
| A | MET314 |
| A | GLY315 |
| A | GLY317 |
| A | LYS318 |
| A | GLU338 |
| A | SER342 |
| A | SER348 |
| A | ARG421 |
| A | HOH4 |
| B | HOH52 |
| B | HOH246 |
| B | LYS500 |
| A | HOH48 |
| A | PHE258 |
| A | LEU259 |
| A | ALA303 |
| A | ILE305 |
| A | LEU306 |
| A | THR307 |
Functional Information from PROSITE/UniProt
| site_id | PS00047 |
| Number of Residues | 5 |
| Details | HISTONE_H4 Histone H4 signature. GAKRH |
| Chain | Residue | Details |
| B | GLY498-HIS502 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| 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_FI2 |
| 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_FI3 |
| 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_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| 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 | 2 |
| Details | M-CSA 525 |
| Chain | Residue | Details |
| A | LEU308 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | SER342 | activator, proton acceptor, proton donor |
