6I6N
Papaver somniferum O-methyltransferase 1
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 | 0009708 | biological_process | benzyl isoquinoline alkaloid biosynthetic process |
| A | 0009820 | biological_process | alkaloid metabolic process |
| A | 0030762 | molecular_function | tetrahydrocolumbamine 2-O-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 | 0009708 | biological_process | benzyl isoquinoline alkaloid biosynthetic process |
| B | 0009820 | biological_process | alkaloid metabolic process |
| B | 0030762 | molecular_function | tetrahydrocolumbamine 2-O-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 | 14 |
| Details | binding site for residue SLX A 401 |
| Chain | Residue |
| A | GLU153 |
| A | LEU347 |
| A | SAH402 |
| A | HOH535 |
| A | HOH602 |
| A | HOH649 |
| A | THR157 |
| A | PHE190 |
| A | PHE203 |
| A | PHE210 |
| A | TRP293 |
| A | HIS296 |
| A | ASN339 |
| A | ILE342 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | binding site for residue SAH A 402 |
| Chain | Residue |
| A | PHE190 |
| A | MET207 |
| A | SER211 |
| A | GLY235 |
| A | GLY237 |
| A | ASP258 |
| A | LEU259 |
| A | VAL262 |
| A | ASP278 |
| A | MET279 |
| A | PHE280 |
| A | LYS292 |
| A | TRP293 |
| A | SLX401 |
| A | HOH511 |
| A | HOH515 |
| A | HOH544 |
| A | HOH594 |
| A | HOH677 |
| A | HOH682 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | binding site for residue SLX B 401 |
| Chain | Residue |
| B | GLU153 |
| B | PHE156 |
| B | PHE190 |
| B | PHE203 |
| B | PHE210 |
| B | TRP293 |
| B | HIS296 |
| B | ASN339 |
| B | ILE342 |
| B | LEU347 |
| B | SAH402 |
| B | HOH539 |
| B | HOH604 |
| B | HOH637 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | binding site for residue SAH B 402 |
| Chain | Residue |
| B | PHE190 |
| B | MET207 |
| B | SER211 |
| B | GLY235 |
| B | GLY237 |
| B | ASP258 |
| B | LEU259 |
| B | VAL262 |
| B | ASP278 |
| B | MET279 |
| B | PHE280 |
| B | LYS292 |
| B | TRP293 |
| B | SLX401 |
| B | HOH511 |
| B | HOH529 |
| B | HOH550 |
| B | HOH587 |
| B | HOH669 |
| B | HOH687 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01020, ECO:0000269|DOI:10.1021/acscatal.9b01038 |
| Chain | Residue | Details |
| A | HIS296 | |
| B | HIS296 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0007744|PDB:6I6K, ECO:0007744|PDB:6I6N |
| Chain | Residue | Details |
| A | GLU153 | |
| B | GLU153 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q5C9L7 |
| Chain | Residue | Details |
| A | MET207 | |
| B | MET207 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|DOI:10.1021/acscatal.9b01038, ECO:0007744|PDB:6I6K, ECO:0007744|PDB:6I6N |
| Chain | Residue | Details |
| A | SER211 | |
| B | HIS296 | |
| A | GLY235 | |
| A | ASP278 | |
| A | LYS292 | |
| A | HIS296 | |
| B | SER211 | |
| B | GLY235 | |
| B | ASP278 | |
| B | LYS292 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01020, ECO:0000269|DOI:10.1021/acscatal.9b01038, ECO:0007744|PDB:6I6K, ECO:0007744|PDB:6I6N |
| Chain | Residue | Details |
| A | ASP258 | |
| B | ASP258 |
