4X3Q
Crystal structure of S-adenosylmethionine-dependent methyltransferase SibL in complex with SAH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008171 | molecular_function | O-methyltransferase activity |
| A | 0046983 | molecular_function | protein dimerization activity |
| A | 1904047 | molecular_function | S-adenosyl-L-methionine binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008171 | molecular_function | O-methyltransferase activity |
| B | 0046983 | molecular_function | protein dimerization activity |
| B | 1904047 | molecular_function | S-adenosyl-L-methionine binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0008168 | molecular_function | methyltransferase activity |
| C | 0008171 | molecular_function | O-methyltransferase activity |
| C | 0046983 | molecular_function | protein dimerization activity |
| C | 1904047 | molecular_function | S-adenosyl-L-methionine binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0008168 | molecular_function | methyltransferase activity |
| D | 0008171 | molecular_function | O-methyltransferase activity |
| D | 0046983 | molecular_function | protein dimerization activity |
| D | 1904047 | molecular_function | S-adenosyl-L-methionine binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue SAH A 401 |
| Chain | Residue |
| A | TYR134 |
| A | ASP201 |
| A | ARG202 |
| A | ALA227 |
| A | ASP228 |
| A | ILE229 |
| A | ALA244 |
| A | HIS245 |
| A | GLN246 |
| A | ILE249 |
| A | TRP250 |
| A | TYR148 |
| A | MSE151 |
| A | SER155 |
| A | GLY178 |
| A | GLY179 |
| A | GLY180 |
| A | VAL183 |
| A | ASN184 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | binding site for residue SAH B 401 |
| Chain | Residue |
| B | TYR134 |
| B | TYR148 |
| B | MSE151 |
| B | SER155 |
| B | GLY178 |
| B | GLY179 |
| B | GLY180 |
| B | VAL183 |
| B | ASN184 |
| B | ASP201 |
| B | ARG202 |
| B | ALA227 |
| B | ASP228 |
| B | ILE229 |
| B | ALA244 |
| B | HIS245 |
| B | GLN246 |
| B | ILE249 |
| B | TRP250 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | binding site for residue SAH C 401 |
| Chain | Residue |
| C | TYR134 |
| C | TYR148 |
| C | MSE151 |
| C | SER155 |
| C | GLY178 |
| C | GLY180 |
| C | ASN184 |
| C | ASP201 |
| C | ARG202 |
| C | ALA227 |
| C | ASP228 |
| C | ILE229 |
| C | ALA244 |
| C | HIS245 |
| C | GLN246 |
| C | ILE249 |
| C | TRP250 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | binding site for residue SAH D 401 |
| Chain | Residue |
| D | TYR134 |
| D | TYR148 |
| D | MSE151 |
| D | SER155 |
| D | GLY178 |
| D | GLY179 |
| D | GLY180 |
| D | VAL183 |
| D | ASN184 |
| D | ASP201 |
| D | ARG202 |
| D | ALA227 |
| D | ASP228 |
| D | ILE229 |
| D | ALA244 |
| D | HIS245 |
| D | GLN246 |
| D | ILE249 |
| D | TRP250 |
