6YJW
Structure of Fragaria ananassa O-methyltransferase crystallized with PAS polypeptide
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 | 0009809 | biological_process | lignin biosynthetic process |
A | 0032259 | biological_process | methylation |
A | 0046983 | molecular_function | protein dimerization activity |
B | 0008168 | molecular_function | methyltransferase activity |
B | 0008171 | molecular_function | O-methyltransferase activity |
B | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
B | 0009809 | biological_process | lignin biosynthetic process |
B | 0032259 | biological_process | methylation |
B | 0046983 | molecular_function | protein dimerization activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | binding site for residue SAH A 401 |
Chain | Residue |
A | MET180 |
A | ASP270 |
A | HOH504 |
A | HOH551 |
A | HOH565 |
A | HOH614 |
A | HOH621 |
A | HOH624 |
A | HOH637 |
A | SER184 |
A | GLY208 |
A | ASP231 |
A | VAL235 |
A | ASP251 |
A | MET252 |
A | LYS265 |
A | ILE267 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue EPE A 402 |
Chain | Residue |
A | ASP164 |
A | ASP251 |
A | HIS275 |
A | LYS278 |
A | HOH567 |
A | HOH575 |
A | HOH590 |
B | GLY167 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue EDO A 403 |
Chain | Residue |
A | LYS37 |
A | GLU41 |
A | ASP133 |
A | LYS134 |
A | ARG171 |
A | HOH511 |
A | HOH535 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue EDO A 404 |
Chain | Residue |
A | ARG79 |
A | ARG82 |
A | ARG104 |
B | LEU300 |
B | HOH544 |
B | HOH567 |
site_id | AC5 |
Number of Residues | 17 |
Details | binding site for residue SAH B 401 |
Chain | Residue |
B | PHE163 |
B | MET180 |
B | SER184 |
B | GLY208 |
B | ASP231 |
B | VAL235 |
B | ASP251 |
B | MET252 |
B | LYS265 |
B | ILE267 |
B | ASP270 |
B | HOH527 |
B | HOH541 |
B | HOH574 |
B | HOH589 |
B | HOH600 |
B | HOH630 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue EPE B 402 |
Chain | Residue |
B | LEU232 |
B | ASP251 |
B | PHE253 |
B | HIS275 |
B | LYS278 |
B | HOH583 |
B | HOH605 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue EDO B 403 |
Chain | Residue |
B | LYS37 |
B | GLU41 |
B | ASP133 |
B | LYS134 |
B | HOH523 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue EDO B 404 |
Chain | Residue |
B | MET130 |
B | LEU136 |
B | PHE176 |
B | HOH576 |
B | HOH588 |
B | HOH596 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue EDO B 405 |
Chain | Residue |
A | LEU300 |
A | HOH545 |
A | HOH592 |
B | ARG79 |
B | ARG82 |
B | HOH612 |
B | HOH652 |