6NEJ
scoulerine 9-O-methyltransferase from Thalictrum flavum complexed (13aS)-3,10-dimethoxy-5,8,13,13a-tetrahydro-6H-isoquino[3,2-a]isoquinoline-2,9-diol and with 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 | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| A | 0030777 | molecular_function | (S)-scoulerine 9-O-methyltransferase activity |
| 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 | 0030777 | molecular_function | (S)-scoulerine 9-O-methyltransferase activity |
| B | 0032259 | biological_process | methylation |
| B | 0046983 | molecular_function | protein dimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue SLX A 401 |
| Chain | Residue |
| A | MET111 |
| A | MET305 |
| A | LEU308 |
| A | ASN309 |
| A | SAH402 |
| B | LEU13 |
| B | GLY14 |
| B | SER16 |
| A | PHE147 |
| A | PHE161 |
| A | TRP251 |
| A | HIS254 |
| A | ASP255 |
| A | PHE283 |
| A | ASN297 |
| A | PRO301 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | binding site for residue SAH A 402 |
| Chain | Residue |
| A | PHE148 |
| A | PHE161 |
| A | MET165 |
| A | SER169 |
| A | GLY193 |
| A | GLU216 |
| A | LEU217 |
| A | VAL220 |
| A | ASN236 |
| A | MET237 |
| A | PHE238 |
| A | LYS250 |
| A | TRP251 |
| A | ASP255 |
| A | SLX401 |
| A | HOH524 |
| A | HOH546 |
| A | HOH586 |
| A | HOH614 |
| A | HOH616 |
| A | HOH636 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | binding site for residue SLX B 401 |
| Chain | Residue |
| A | LEU13 |
| A | GLY14 |
| A | SER16 |
| B | MET111 |
| B | PHE114 |
| B | PHE147 |
| B | PHE161 |
| B | TRP251 |
| B | HIS254 |
| B | ASP255 |
| B | ASN297 |
| B | PRO301 |
| B | MET305 |
| B | ASN309 |
| B | SAH402 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | binding site for residue SAH B 402 |
| Chain | Residue |
| B | PHE148 |
| B | PHE161 |
| B | MET165 |
| B | SER169 |
| B | GLY193 |
| B | GLU216 |
| B | LEU217 |
| B | VAL220 |
| B | ASN236 |
| B | MET237 |
| B | PHE238 |
| B | LYS250 |
| B | TRP251 |
| B | ASP255 |
| B | SLX401 |
| B | HOH524 |
| B | HOH545 |
| B | HOH564 |
| B | HOH586 |
| B | HOH618 |
| B | HOH681 |
