1ZGA
Crystal structure of isoflavanone 4'-O-methyltransferase complexed with (+)-6a-hydroxymaackiain
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008168 | molecular_function | methyltransferase activity |
A | 0008171 | molecular_function | O-methyltransferase activity |
A | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
A | 0019438 | biological_process | obsolete aromatic compound biosynthetic process |
A | 0030746 | molecular_function | isoflavone 4'-O-methyltransferase activity |
A | 0032259 | biological_process | methylation |
A | 0046983 | molecular_function | protein dimerization activity |
A | 0102670 | molecular_function | 2,7,4'-trihydroxyisoflavanone-4'-O-methyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE HMK A 365 |
Chain | Residue |
A | TYR25 |
A | MET322 |
A | MET325 |
A | GLY125 |
A | SER130 |
A | SER131 |
A | PHE159 |
A | MET174 |
A | PHE175 |
A | ASP182 |
A | TYR318 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SAH A 3994 |
Chain | Residue |
A | GLY207 |
A | VAL213 |
A | ASP230 |
A | GLN231 |
A | ASP250 |
A | MET251 |
A | PHE252 |
A | LYS264 |
A | TRP265 |
A | HOH3997 |
A | HOH4109 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01020 |
Chain | Residue | Details |
A | HIS268 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP250 | |
A | LYS264 | |
A | VAL206 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01020 |
Chain | Residue | Details |
A | ASP230 |