3P9K
Crystal structure of perennial ryegrass LpOMT1 complexed with S-adenosyl-L-homocysteine and coniferaldehyde
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 | 0016206 | molecular_function | catechol 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 | 0016206 | molecular_function | catechol O-methyltransferase 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 | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
C | 0016206 | molecular_function | catechol O-methyltransferase 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 | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
D | 0016206 | molecular_function | catechol O-methyltransferase 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 | PHE250 |
A | LYS262 |
A | ILE264 |
A | ASP267 |
A | CIY601 |
A | HOH1027 |
A | HOH1054 |
A | HOH1199 |
A | HOH1203 |
A | HOH1331 |
A | SER181 |
A | GLY205 |
A | GLY207 |
A | ASP228 |
A | LEU229 |
A | VAL232 |
A | ASP248 |
A | MET249 |
site_id | AC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE SAH B 402 |
Chain | Residue |
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 | ASP267 |
B | CIY602 |
B | HOH1067 |
B | HOH1183 |
B | HOH1205 |
site_id | AC3 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE SAH C 403 |
Chain | Residue |
C | MET177 |
C | SER181 |
C | GLY205 |
C | GLY207 |
C | ASP228 |
C | LEU229 |
C | ASP248 |
C | MET249 |
C | LYS262 |
C | ASP267 |
C | CIY603 |
C | HOH1003 |
C | HOH1036 |
C | HOH1245 |
C | HOH1261 |
C | HOH1324 |
C | HOH1637 |
site_id | AC4 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE SAH D 404 |
Chain | Residue |
D | PHE160 |
D | MET177 |
D | SER181 |
D | GLY205 |
D | GLY207 |
D | ASP228 |
D | VAL232 |
D | ASP248 |
D | MET249 |
D | PHE250 |
D | LYS262 |
D | ASP267 |
D | CIY604 |
D | HOH1017 |
D | HOH1049 |
D | HOH1338 |
D | HOH1395 |
site_id | AC5 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE CIY A 601 |
Chain | Residue |
A | MET127 |
A | ASN128 |
A | MET177 |
A | TRP263 |
A | HIS266 |
A | ASP267 |
A | ILE316 |
A | MET317 |
A | ASN321 |
A | SAH401 |
A | HOH1101 |
B | SER25 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE CIY B 602 |
Chain | Residue |
B | MET127 |
B | ASN128 |
B | PHE173 |
B | TRP263 |
B | HIS266 |
B | ASP267 |
B | MET317 |
B | ASN321 |
B | SAH402 |
B | HOH1115 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE CIY C 603 |
Chain | Residue |
C | SAH403 |
C | HOH1062 |
C | MET127 |
C | ASN128 |
C | TRP263 |
C | HIS266 |
C | ASP267 |
C | MET317 |
C | ASN321 |
site_id | AC8 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE CIY D 604 |
Chain | Residue |
D | MET127 |
D | ASN128 |
D | PHE173 |
D | TRP263 |
D | HIS266 |
D | ASP267 |
D | MET317 |
D | ASN321 |
D | SAH404 |
D | HOH1089 |
D | HOH1480 |
Functional Information from PROSITE/UniProt
site_id | PS00012 |
Number of Residues | 16 |
Details | PHOSPHOPANTETHEINE Phosphopantetheine attachment site. AAGGKSLTPTEVAAKL |
Chain | Residue | Details |
A | ALA47-LEU62 |