3BGD
Thiopurine S-Methyltransferase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006805 | biological_process | xenobiotic metabolic process |
| A | 0008119 | molecular_function | thiopurine S-methyltransferase activity |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0032259 | biological_process | methylation |
| A | 1904047 | molecular_function | S-adenosyl-L-methionine binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006805 | biological_process | xenobiotic metabolic process |
| B | 0008119 | molecular_function | thiopurine S-methyltransferase activity |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0032259 | biological_process | methylation |
| B | 1904047 | molecular_function | S-adenosyl-L-methionine binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE SAH A 300 |
| Chain | Residue |
| A | LEU21 |
| A | SER129 |
| A | ILE130 |
| A | ARG147 |
| A | GLY148 |
| A | HOH310 |
| A | HOH321 |
| A | HOH323 |
| A | HOH336 |
| A | TRP24 |
| A | TRP28 |
| A | PHE35 |
| A | LEU64 |
| A | CYS65 |
| A | GLU85 |
| A | ILE86 |
| A | CYS128 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE SAH B 300 |
| Chain | Residue |
| B | LEU21 |
| B | TRP24 |
| B | TRP28 |
| B | PHE35 |
| B | LEU64 |
| B | CYS65 |
| B | GLU85 |
| B | ILE86 |
| B | CYS128 |
| B | SER129 |
| B | ILE130 |
| B | ARG147 |
| B | GLY148 |
| B | HOH310 |
| B | HOH322 |
| B | HOH381 |
| B | HOH394 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PM6 A 301 |
| Chain | Residue |
| A | PHE35 |
| A | ARG147 |
| A | GLY148 |
| A | ALA152 |
| A | PRO191 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PM6 A 302 |
| Chain | Residue |
| A | HIS47 |
| A | THR50 |
| A | PHE51 |
| A | GLN174 |
| A | LEU212 |
| A | LEU236 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PM6 B 301 |
| Chain | Residue |
| B | PHE35 |
| B | ARG147 |
| B | GLY148 |
| B | PRO191 |
| B | ARG221 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PM6 B 302 |
| Chain | Residue |
| B | HIS47 |
| B | THR50 |
| B | GLN174 |
| B | LEU212 |
| B | LEU236 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 32 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P51580","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
