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 |