2H11
Amino-terminal Truncated Thiopurine S-Methyltransferase Complexed with S-Adenosyl-L-Homocysteine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| 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 | 0032259 | biological_process | methylation |
| A | 0042178 | biological_process | xenobiotic catabolic process |
| A | 1904047 | molecular_function | S-adenosyl-L-methionine binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| 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 | 0032259 | biological_process | methylation |
| B | 0042178 | biological_process | xenobiotic catabolic process |
| B | 1904047 | molecular_function | S-adenosyl-L-methionine binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SCN A 4 |
| Chain | Residue |
| A | GLU110 |
| A | PRO111 |
| A | HOH447 |
| B | ARG215 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SCN B 5 |
| Chain | Residue |
| A | ARG215 |
| B | GLU110 |
| B | PRO111 |
| B | HOH457 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SCN B 6 |
| Chain | Residue |
| B | LYS122 |
| B | SER129 |
| B | TYR131 |
| B | ARG64 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SCN A 7 |
| Chain | Residue |
| A | B3P1 |
| A | ARG64 |
| A | SER129 |
| A | TYR131 |
| A | HOH386 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE SAH A 300 |
| Chain | Residue |
| A | LEU26 |
| A | TRP29 |
| A | TRP33 |
| A | PHE40 |
| A | LEU69 |
| A | CYS70 |
| A | GLU90 |
| A | ILE91 |
| A | CYS133 |
| A | SER134 |
| A | ILE135 |
| A | ARG152 |
| A | GLY153 |
| A | HOH309 |
| A | HOH315 |
| A | HOH319 |
| A | HOH379 |
| A | HOH385 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE SAH B 301 |
| Chain | Residue |
| B | LEU26 |
| B | TRP29 |
| B | TRP33 |
| B | PHE40 |
| B | LEU69 |
| B | CYS70 |
| B | GLU90 |
| B | ILE91 |
| B | CYS133 |
| B | SER134 |
| B | ILE135 |
| B | ARG152 |
| B | GLY153 |
| B | HOH313 |
| B | HOH319 |
| B | HOH323 |
| B | HOH382 |
| B | HOH387 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE B3P A 1 |
| Chain | Residue |
| A | SCN7 |
| A | ARG64 |
| A | PRO111 |
| A | ILE112 |
| A | THR113 |
| A | GLU114 |
| A | TYR131 |
| A | ASN142 |
| A | ILE143 |
| A | HOH350 |
| A | HOH397 |
| A | HOH402 |
| A | HOH403 |
| A | HOH439 |
| B | LYS228 |
| B | SER229 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE B3P B 2 |
| Chain | Residue |
| A | LYS228 |
| A | SER229 |
| B | ARG64 |
| B | PRO111 |
| B | ILE112 |
| B | THR113 |
| B | GLU114 |
| B | LYS122 |
| B | TYR131 |
| B | THR141 |
| B | ASN142 |
| B | ILE143 |
| B | HOH354 |
| B | HOH396 |
| B | HOH400 |
| B | HOH401 |
| B | HOH437 |
| B | HOH438 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE B3P A 3 |
| Chain | Residue |
| A | ILE115 |
| A | SER134 |
| A | ASP137 |
| A | HOH415 |
| A | HOH435 |
| B | ILE115 |
| B | ASP137 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | TRP29 | |
| B | ARG152 | |
| A | LEU69 | |
| A | GLU90 | |
| A | SER134 | |
| A | ARG152 | |
| B | TRP29 | |
| B | LEU69 | |
| B | GLU90 | |
| B | SER134 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | PHE40 | |
| B | PHE40 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS58 | |
| B | LYS58 |
