3P9I
Crystal structure of perennial ryegrass LpOMT1 complexed with S-adenosyl-L-homocysteine and sinapaldehyde
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008171 | molecular_function | O-methyltransferase activity |
| A | 0009813 | biological_process | flavonoid biosynthetic process |
| A | 0016206 | molecular_function | catechol O-methyltransferase activity |
| A | 0016740 | molecular_function | transferase 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 | 0009813 | biological_process | flavonoid biosynthetic process |
| B | 0016206 | molecular_function | catechol O-methyltransferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0032259 | biological_process | methylation |
| B | 0046983 | molecular_function | protein dimerization activity |
| C | 0008168 | molecular_function | methyltransferase activity |
| C | 0008171 | molecular_function | O-methyltransferase activity |
| C | 0009813 | biological_process | flavonoid biosynthetic process |
| C | 0016206 | molecular_function | catechol O-methyltransferase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0032259 | biological_process | methylation |
| C | 0046983 | molecular_function | protein dimerization activity |
| D | 0008168 | molecular_function | methyltransferase activity |
| D | 0008171 | molecular_function | O-methyltransferase activity |
| D | 0009813 | biological_process | flavonoid biosynthetic process |
| D | 0016206 | molecular_function | catechol O-methyltransferase activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0032259 | biological_process | methylation |
| D | 0046983 | molecular_function | protein dimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE SAH A 401 |
| Chain | Residue |
| A | MET177 |
| A | LYS262 |
| A | ASP267 |
| A | TRP268 |
| A | SNY601 |
| A | HOH1027 |
| A | HOH1054 |
| A | HOH1083 |
| A | HOH1199 |
| A | HOH1203 |
| A | HOH1331 |
| A | SER181 |
| A | GLY205 |
| A | GLY207 |
| A | ASP228 |
| A | LEU229 |
| A | ASP248 |
| A | MET249 |
| A | PHE250 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SNY A 601 |
| Chain | Residue |
| A | ASN128 |
| A | LEU133 |
| A | TRP263 |
| A | HIS266 |
| A | ASP267 |
| A | MET317 |
| A | ASN321 |
| A | SAH401 |
| A | HOH1101 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BME A 1089 |
| Chain | Residue |
| A | CYS89 |
| A | VAL91 |
| A | ARG101 |
| A | TYR103 |
| A | HOH1425 |
| A | HOH1429 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BME A 1295 |
| Chain | Residue |
| A | CYS295 |
| A | GLY309 |
| A | VAL313 |
| A | ASN352 |
| B | LEU21 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE SAH B 402 |
| Chain | Residue |
| B | PHE173 |
| B | MET177 |
| B | SER181 |
| B | GLY205 |
| B | GLY207 |
| B | ASP228 |
| B | LEU229 |
| B | VAL232 |
| B | GLY247 |
| B | ASP248 |
| B | MET249 |
| B | LYS262 |
| B | ILE264 |
| B | SNY602 |
| B | HOH1067 |
| B | HOH1143 |
| B | HOH1182 |
| B | HOH1183 |
| B | HOH1205 |
| B | HOH1489 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SNY B 602 |
| Chain | Residue |
| B | ASN128 |
| B | LEU133 |
| B | PHE173 |
| B | TRP263 |
| B | HIS266 |
| B | ASP267 |
| B | MET317 |
| B | ASN321 |
| B | SAH402 |
| B | HOH1115 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BME B 2089 |
| Chain | Residue |
| A | PRO301 |
| A | HOH1256 |
| B | CYS89 |
| B | LEU90 |
| B | VAL91 |
| B | HOH1319 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME B 2295 |
| Chain | Residue |
| A | LEU21 |
| B | CYS295 |
| B | VAL313 |
| site_id | AC9 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE SAH C 403 |
| Chain | Residue |
| C | MET177 |
| C | SER181 |
| C | GLY205 |
| C | GLY207 |
| C | ASP228 |
| C | LEU229 |
| C | VAL232 |
| C | ASP248 |
| C | MET249 |
| C | PHE250 |
| C | LYS262 |
| C | SNY603 |
| C | HOH1003 |
| C | HOH1036 |
| C | HOH1245 |
| C | HOH1261 |
| C | HOH1324 |
| C | HOH1584 |
| C | HOH1637 |
| site_id | BC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SNY C 603 |
| Chain | Residue |
| C | LEU133 |
| C | TRP263 |
| C | HIS266 |
| C | ASP267 |
| C | MET317 |
| C | ASN321 |
| C | SAH403 |
| C | HOH1062 |
| D | HOH1308 |
| C | MET127 |
| C | ASN128 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE BME C 3089 |
| Chain | Residue |
| C | ARG79 |
| C | CYS89 |
| C | ARG101 |
| C | TYR103 |
| C | HOH1265 |
| D | PRO301 |
| D | HOH1312 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BME C 3295 |
| Chain | Residue |
| C | CYS295 |
| C | GLY309 |
| C | VAL310 |
| C | VAL313 |
| C | ASN352 |
| site_id | BC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE SAH D 404 |
| Chain | Residue |
| D | PHE160 |
| D | MET177 |
| D | SER181 |
| D | GLY205 |
| D | GLY207 |
| D | ASP228 |
| D | LEU229 |
| D | VAL232 |
| D | GLY247 |
| D | ASP248 |
| D | MET249 |
| D | PHE250 |
| D | LYS262 |
| D | SNY604 |
| D | HOH1017 |
| D | HOH1049 |
| D | HOH1071 |
| D | HOH1100 |
| D | HOH1193 |
| D | HOH1395 |
| D | HOH1704 |
| site_id | BC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SNY D 604 |
| Chain | Residue |
| C | HOH1480 |
| D | MET127 |
| D | ASN128 |
| D | LEU133 |
| D | TRP263 |
| D | HIS266 |
| D | ASP267 |
| D | MET317 |
| D | ASN321 |
| D | SAH404 |
| D | HOH1089 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BME D 4089 |
| Chain | Residue |
| C | PHE311 |
| C | HOH1124 |
| D | ARG79 |
| D | CYS89 |
| D | LEU90 |
| D | VAL91 |
| D | ARG101 |
| D | HOH1129 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BME D 4295 |
| Chain | Residue |
| C | LEU21 |
| D | CYS295 |
| D | GLY309 |
| D | VAL310 |
| D | VAL313 |
| D | HOH1464 |
Functional Information from PROSITE/UniProt
| site_id | PS00012 |
| Number of Residues | 16 |
| Details | PHOSPHOPANTETHEINE Phosphopantetheine attachment site. AAGGKSLTPTEVAAKL |
| Chain | Residue | Details |
| A | ALA47-LEU62 |
