3TVL
Complex between the human thiamine triphosphatase and triphosphate
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 | 13 |
Details | BINDING SITE FOR RESIDUE 3PO A 231 |
Chain | Residue |
A | LYS11 |
A | HOH243 |
A | HOH252 |
A | HOH254 |
A | HOH287 |
A | TYR39 |
A | ARG55 |
A | ARG57 |
A | LYS65 |
A | ARG125 |
A | GLU157 |
A | LYS193 |
A | HOH242 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 232 |
Chain | Residue |
A | TYR39 |
A | TYR40 |
A | LEU47 |
A | HIS52 |
A | TRP53 |
A | LEU54 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 3PO B 231 |
Chain | Residue |
B | LYS11 |
B | TYR39 |
B | ARG55 |
B | ARG57 |
B | LYS65 |
B | GLU81 |
B | ARG125 |
B | GLU157 |
B | ALA192 |
B | LYS193 |
B | HOH238 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 232 |
Chain | Residue |
A | PHE201 |
B | ARG36 |
B | THR38 |
B | ARG56 |
B | GLU58 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO B 233 |
Chain | Residue |
B | TYR39 |
B | TYR40 |
B | ASP41 |
B | LEU47 |
B | MET48 |
B | HIS52 |
B | TRP53 |
B | LEU54 |
B | LEU194 |
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 |