4YMH
Crystal structure of SAH-bound Podospora anserina methyltransferase PaMTH1
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 | 0016740 | molecular_function | transferase activity |
| A | 0032259 | biological_process | methylation |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008171 | molecular_function | O-methyltransferase activity |
| B | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0032259 | biological_process | methylation |
| C | 0008168 | molecular_function | methyltransferase activity |
| C | 0008171 | molecular_function | O-methyltransferase activity |
| C | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0032259 | biological_process | methylation |
| D | 0008168 | molecular_function | methyltransferase activity |
| D | 0008171 | molecular_function | O-methyltransferase activity |
| D | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0032259 | biological_process | methylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | binding site for residue SAH A 1001 |
| Chain | Residue |
| A | LYS47 |
| A | GLU128 |
| A | ASP144 |
| A | ALA145 |
| A | ASN146 |
| A | TYR153 |
| A | HOH1118 |
| A | HOH1159 |
| A | HOH1285 |
| A | MET48 |
| A | SER49 |
| A | GLY73 |
| A | TYR75 |
| A | SER79 |
| A | GLU98 |
| A | TYR99 |
| A | ALA127 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue PEG A 1002 |
| Chain | Residue |
| A | ARG64 |
| A | ASN166 |
| B | ASP63 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | binding site for residue SAH B 1001 |
| Chain | Residue |
| B | MET48 |
| B | SER49 |
| B | GLY73 |
| B | TYR75 |
| B | SER79 |
| B | GLU98 |
| B | TYR99 |
| B | ALA127 |
| B | GLU128 |
| B | ASP144 |
| B | ALA145 |
| B | ASN146 |
| B | TYR153 |
| B | HOH1134 |
| B | HOH1175 |
| B | HOH1266 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue PEG B 1002 |
| Chain | Residue |
| B | TRP233 |
| B | HOH1263 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue PEG B 1003 |
| Chain | Residue |
| B | ASP46 |
| B | LYS47 |
| B | HOH1324 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | binding site for residue SAH C 1001 |
| Chain | Residue |
| B | LYS102 |
| C | LYS47 |
| C | MET48 |
| C | SER49 |
| C | GLY73 |
| C | TYR75 |
| C | SER79 |
| C | GLU98 |
| C | TYR99 |
| C | PRO126 |
| C | ALA127 |
| C | GLU128 |
| C | ASP144 |
| C | ALA145 |
| C | ASN146 |
| C | TYR153 |
| C | HOH1111 |
| C | HOH1153 |
| C | HOH1250 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | binding site for residue SAH D 1001 |
| Chain | Residue |
| D | LYS47 |
| D | MET48 |
| D | SER49 |
| D | GLY73 |
| D | TYR75 |
| D | TYR78 |
| D | SER79 |
| D | GLU98 |
| D | TYR99 |
| D | ALA127 |
| D | GLU128 |
| D | ASP144 |
| D | ALA145 |
| D | ASN146 |
| D | TYR153 |
| D | HOH1107 |
| D | HOH1111 |
| D | HOH1134 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue PEG D 1002 |
| Chain | Residue |
| C | ARG64 |
| D | ARG64 |
| D | HOH1234 |
