3BHD
Crystal structure of human thiamine triphosphatase (THTPA)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006091 | biological_process | generation of precursor metabolites and energy |
| A | 0006772 | biological_process | thiamine metabolic process |
| A | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
| A | 0016311 | biological_process | dephosphorylation |
| A | 0016462 | molecular_function | pyrophosphatase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0042357 | biological_process | thiamine diphosphate metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050333 | molecular_function | thiamine triphosphate phosphatase activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006091 | biological_process | generation of precursor metabolites and energy |
| B | 0006772 | biological_process | thiamine metabolic process |
| B | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
| B | 0016311 | biological_process | dephosphorylation |
| B | 0016462 | molecular_function | pyrophosphatase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0042357 | biological_process | thiamine diphosphate metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050333 | molecular_function | thiamine triphosphate phosphatase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 216 |
| Chain | Residue |
| A | ARG57 |
| A | LYS65 |
| A | ARG125 |
| A | CIT219 |
| A | HOH295 |
| A | HOH296 |
| A | HOH297 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 218 |
| Chain | Residue |
| A | CIT219 |
| A | HOH268 |
| A | ALA192 |
| A | LYS193 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA B 216 |
| Chain | Residue |
| B | CIT217 |
| B | CIT218 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CIT A 219 |
| Chain | Residue |
| A | GLU9 |
| A | LYS11 |
| A | TYR39 |
| A | LYS65 |
| A | HIS76 |
| A | TYR79 |
| A | ALA192 |
| A | SO4216 |
| A | CL218 |
| A | HOH252 |
| A | HOH293 |
| A | HOH296 |
| A | HOH297 |
| A | HOH298 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE CIT B 217 |
| Chain | Residue |
| B | GLU9 |
| B | LYS11 |
| B | TYR39 |
| B | TRP53 |
| B | ARG55 |
| B | LYS65 |
| B | HIS76 |
| B | TYR79 |
| B | ALA192 |
| B | NA216 |
| B | CIT218 |
| B | HOH358 |
| B | HOH406 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CIT B 218 |
| Chain | Residue |
| B | LYS11 |
| B | TYR39 |
| B | ARG55 |
| B | ARG57 |
| B | LYS65 |
| B | ARG125 |
| B | GLU157 |
| B | ALA192 |
| B | LYS193 |
| B | NA216 |
| B | CIT217 |
| B | HOH406 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 219 |
| Chain | Residue |
| A | ASP150 |
| A | ARG200 |
| B | THR34 |
| B | GLU58 |
| B | HOH336 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 220 |
| Chain | Residue |
| B | TYR31 |
| B | ARG57 |
| B | GLU58 |
| B | ASP59 |
| B | SER60 |
| B | ARG125 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 221 |
| Chain | Residue |
| B | PHE12 |
| B | LEU13 |
| B | SER179 |
| B | SER180 |
| B | GLY183 |
| B | VAL184 |
| B | HOH353 |
| B | HOH423 |
| B | HOH426 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 222 |
| Chain | Residue |
| B | TRP53 |
| B | HIS76 |
| B | HOH383 |
| B | HOH394 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 223 |
| Chain | Residue |
| B | GLU19 |
| B | LYS124 |
| B | SER126 |
| B | LEU146 |
| B | ASP147 |
| B | THR148 |
| B | HOH399 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU7 | |
| A | GLU9 | |
| A | ASP145 | |
| A | GLU159 | |
| B | GLU7 | |
| B | GLU9 | |
| B | ASP145 | |
| B | GLU159 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS11 | |
| B | LYS65 | |
| B | ARG125 | |
| B | GLU157 | |
| A | ARG55 | |
| A | ARG57 | |
| A | LYS65 | |
| A | ARG125 | |
| A | GLU157 | |
| B | LYS11 | |
| B | ARG55 | |
| B | ARG57 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| A | LYS193 | |
| B | LYS193 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378 |
| Chain | Residue | Details |
| A | ALA2 | |
| B | ALA2 |
