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 | 0009058 | biological_process | biosynthetic process |
A | 0032259 | biological_process | methylation |
B | 0008168 | molecular_function | methyltransferase activity |
B | 0008171 | molecular_function | O-methyltransferase activity |
B | 0009058 | biological_process | biosynthetic process |
B | 0032259 | biological_process | methylation |
C | 0008168 | molecular_function | methyltransferase activity |
C | 0008171 | molecular_function | O-methyltransferase activity |
C | 0009058 | biological_process | biosynthetic process |
C | 0032259 | biological_process | methylation |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01020 |
Chain | Residue | Details |
A | HIS373 | |
B | HIS373 | |
C | HIS373 |
site_id | SWS_FT_FI2 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:O04385 |
Chain | Residue | Details |
A | GLY298 | |
A | SER353 | |
A | ARG369 | |
B | GLY298 | |
B | SER353 | |
B | ARG369 | |
C | GLY298 | |
C | SER353 | |
C | ARG369 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01020 |
Chain | Residue | Details |
A | ASP321 | |
B | ASP321 | |
C | ASP321 |