1MUF
Structure of histone H3 K4-specific methyltransferase SET7/9
Functional Information from GO Data
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 22 |
Details | Repeat: {"description":"MORN 3"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"12514135","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12540855","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | Site: {"description":"Histone H3K4 binding","evidences":[{"source":"PubMed","id":"12540855","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1h3i |
Chain | Residue | Details |
A | TYR335 | |
A | HIS293 |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 350 |
Chain | Residue | Details |
A | ASN265 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
A | PHE313 | electrostatic stabiliser, hydrogen bond acceptor |
A | LYS317 | electrostatic stabiliser, hydrogen bond acceptor |
A | VAL325 | activator, electrostatic stabiliser, hydrogen bond acceptor |