6NEH
N191D, F205S mutant of scoulerine 9-O-methyltransferase from Thalictrum flavum complexed with (13aS)-3,10-dimethoxy-5,8,13,13a-tetrahydro-6H-isoquino[3,2-a]isoquinoline-2,9-diol 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 | 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 | 23 |
Details | binding site for residue SAH A 401 |
Chain | Residue |
A | PHE148 |
A | ASN236 |
A | MET237 |
A | PHE238 |
A | LYS250 |
A | TRP251 |
A | ASP255 |
A | SLX402 |
A | HOH539 |
A | HOH540 |
A | HOH549 |
A | PHE161 |
A | HOH597 |
A | HOH608 |
A | HOH619 |
A | HOH630 |
A | MET165 |
A | SER169 |
A | GLY193 |
A | GLU216 |
A | LEU217 |
A | VAL220 |
A | GLY235 |
site_id | AC2 |
Number of Residues | 15 |
Details | binding site for residue SLX A 402 |
Chain | Residue |
A | MET111 |
A | PHE147 |
A | PHE161 |
A | TRP251 |
A | HIS254 |
A | ASP255 |
A | PHE283 |
A | ASN297 |
A | PRO301 |
A | MET305 |
A | ASN309 |
A | SAH401 |
B | LEU13 |
B | GLY14 |
B | SER16 |
site_id | AC3 |
Number of Residues | 23 |
Details | binding site for residue SAH B 401 |
Chain | Residue |
B | PHE148 |
B | PHE161 |
B | MET165 |
B | SER169 |
B | GLY193 |
B | GLU216 |
B | LEU217 |
B | VAL220 |
B | GLY235 |
B | ASN236 |
B | MET237 |
B | PHE238 |
B | LYS250 |
B | TRP251 |
B | ASP255 |
B | SLX402 |
B | HOH518 |
B | HOH539 |
B | HOH552 |
B | HOH598 |
B | HOH599 |
B | HOH603 |
B | HOH618 |
site_id | AC4 |
Number of Residues | 15 |
Details | binding site for residue SLX B 402 |
Chain | Residue |
A | LEU13 |
A | GLY14 |
A | SER16 |
B | MET111 |
B | PHE147 |
B | PHE161 |
B | TRP251 |
B | HIS254 |
B | ASP255 |
B | PHE283 |
B | ASN297 |
B | PRO301 |
B | MET305 |
B | ASN309 |
B | SAH401 |