7WH9
holo structure of emodin 1-OH O-methyltransferase complex with emodin and S-Adenosyl-L-homocysteine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008171 | molecular_function | O-methyltransferase activity |
| A | 0044550 | biological_process | secondary metabolite biosynthetic process |
| A | 0046983 | molecular_function | protein dimerization activity |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008171 | molecular_function | O-methyltransferase activity |
| B | 0044550 | biological_process | secondary metabolite biosynthetic process |
| B | 0046983 | molecular_function | protein dimerization activity |
| C | 0008168 | molecular_function | methyltransferase activity |
| C | 0008171 | molecular_function | O-methyltransferase activity |
| C | 0044550 | biological_process | secondary metabolite biosynthetic process |
| C | 0046983 | molecular_function | protein dimerization activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01020","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"35475366","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"35475366","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"35475366","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7WH9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
