2PQ8
MYST histone acetyltransferase 1
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 501 |
| Chain | Residue |
| A | CYS210 |
| A | CYS213 |
| A | HIS226 |
| A | CYS230 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE COA A 601 |
| Chain | Residue |
| A | HOH113 |
| A | HOH121 |
| A | HOH122 |
| A | HOH144 |
| A | PHE270 |
| A | LEU271 |
| A | ILE317 |
| A | LEU318 |
| A | THR319 |
| A | GLN324 |
| A | ARG325 |
| A | ARG326 |
| A | GLY327 |
| A | GLY329 |
| A | LYS330 |
| A | SER354 |
| A | LEU356 |
| A | LEU359 |
| A | SER360 |
| A | SER363 |
| A | UNX701 |
| A | HOH13 |
| A | HOH23 |
| A | HOH24 |
| A | HOH50 |
| A | HOH103 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNX A 701 |
| Chain | Residue |
| A | ILE317 |
| A | COA601 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE UNX A 702 |
| Chain | Residue |
| A | HIS297 |
| A | ILE298 |
| A | TYR323 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE UNX A 703 |
| Chain | Residue |
| A | LYS215 |
| A | ILE258 |
| A | ASN262 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE UNX A 704 |
| Chain | Residue |
| A | GLU239 |
| A | ARG274 |
| A | THR275 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE UNX A 705 |
| Chain | Residue |
| A | HOH30 |
| A | TYR219 |
| A | GLU220 |
| A | LYS221 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNX A 706 |
| Chain | Residue |
| A | ARG233 |
| A | GLN234 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNX A 707 |
| Chain | Residue |
| A | GLU250 |
| A | ASP252 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNX A 708 |
| Chain | Residue |
| A | PHE283 |
| A | PHE285 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNX A 709 |
| Chain | Residue |
| A | TYR187 |
| A | GLU188 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNX A 710 |
| Chain | Residue |
| A | HOH14 |
| A | ASP190 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE UNX A 711 |
| Chain | Residue |
| A | PRO236 |
| A | GLY237 |
| A | HIS256 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE UNX A 712 |
| Chain | Residue |
| A | HOH55 |
| A | GLY185 |
| A | LEU209 |
| A | GLU211 |
| A | TYR223 |
| site_id | BC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNX A 713 |
| Chain | Residue |
| A | GLN393 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 25 |
| Details | Zinc finger: {"description":"C2HC MYST-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01063","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"21217699","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"27768893","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"33657400","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21217699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21691301","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27382063","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29321206","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2007","submissionDatabase":"PDB data bank","title":"MYST histone acetyltransferase 1.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2GIV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PQ8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Y0M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QAH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TOA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TOB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4DNC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J8C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J8F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5WCI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29321206","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5WCI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21217699","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2007","submissionDatabase":"PDB data bank","title":"MYST histone acetyltransferase 1.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2GIV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Y0M","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21217699","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2Y0M","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"21217699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21691301","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22547026","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22918831","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27382063","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2007","submissionDatabase":"PDB data bank","title":"MYST histone acetyltransferase 1.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2GIV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| 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 | GLU350 | |
| A | CYS316 |






