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 | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12514135, ECO:0000269|PubMed:12540855 |
Chain | Residue | Details |
A | ALA226 | |
A | ASN296 | |
A | HIS297 |
site_id | SWS_FT_FI2 |
Number of Residues | 5 |
Details | SITE: Histone H3K4 binding => ECO:0000269|PubMed:12540855 |
Chain | Residue | Details |
A | TYR245 | |
A | ASP256 | |
A | THR266 | |
A | LYS317 | |
A | TYR335 |
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 | 5 |
Details | M-CSA 350 |
Chain | Residue | Details |
A | TYR245 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
A | HIS293 | electrostatic stabiliser, hydrogen bond acceptor |
A | HIS297 | electrostatic stabiliser, hydrogen bond acceptor |
A | TYR305 | activator, electrostatic stabiliser, hydrogen bond acceptor |
A | TYR335 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |