5A64
Crystal structure of mouse thiamine triphosphatase in complex with thiamine triphosphate.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| 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 | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| 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 | 23 |
| Details | BINDING SITE FOR RESIDUE V4E A 1000 |
| Chain | Residue |
| A | GLU9 |
| A | ARG125 |
| A | GLU157 |
| A | GLU159 |
| A | ALA192 |
| A | LYS193 |
| A | HOH2001 |
| A | HOH2002 |
| A | HOH2006 |
| A | HOH2023 |
| A | HOH2038 |
| A | LYS11 |
| A | HOH2064 |
| A | HOH2075 |
| A | HOH2076 |
| A | HOH2077 |
| A | TYR39 |
| A | ASP51 |
| A | TRP53 |
| A | ARG55 |
| A | ARG57 |
| A | LYS65 |
| A | TYR79 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE V4E B 1000 |
| Chain | Residue |
| B | GLU9 |
| B | LYS11 |
| B | TYR39 |
| B | ASP51 |
| B | TRP53 |
| B | ARG55 |
| B | ARG57 |
| B | LYS65 |
| B | ASN77 |
| B | TYR79 |
| B | ARG125 |
| B | GLU157 |
| B | GLU159 |
| B | ALA192 |
| B | LYS193 |
| B | HOH2001 |
| B | HOH2003 |
| B | HOH2011 |
| B | HOH2012 |
| B | HOH2017 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 1216 |
| Chain | Residue |
| A | THR124 |
| A | SER148 |
| A | ASP150 |
| A | EDO1219 |
| B | GLU117 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1217 |
| Chain | Residue |
| A | SER60 |
| A | GLY61 |
| A | TRP62 |
| A | THR83 |
| A | GLU85 |
| A | HOH2088 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 1218 |
| Chain | Residue |
| A | GLU58 |
| A | GLY59 |
| A | SER60 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 1219 |
| Chain | Residue |
| A | ASP150 |
| A | EDO1216 |
| B | SER120 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PGE A 1220 |
| Chain | Residue |
| A | THR38 |
| A | GLU117 |
| A | SER120 |
| A | PRO203 |
| A | LEU204 |
| A | GLN207 |
| A | PGE1221 |
| A | HOH2089 |
| A | HOH2090 |
| B | HOH2042 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PGE A 1221 |
| Chain | Residue |
| A | ARG36 |
| A | ASP37 |
| A | THR38 |
| A | GLN56 |
| A | GLU58 |
| A | PGE1220 |
| A | HOH2090 |
| B | ARG36 |
| B | ILE122 |
| B | ASP150 |
| B | HOH2010 |
| B | HOH2042 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | BINDING: |
| Chain | Residue | Details |
| B | GLU7 | |
| B | GLU9 | |
| B | LYS11 | |
| B | ARG55 | |
| B | ARG57 | |
| B | LYS65 | |
| B | ARG125 | |
| B | ASP145 | |
| B | GLU159 | |
| B | LYS193 | |
| A | LYS11 | |
| A | ARG55 | |
| A | ARG57 | |
| A | LYS65 | |
| A | ARG125 | |
| A | ASP145 | |
| A | GLU159 | |
| A | LYS193 | |
| A | GLU7 | |
| A | GLU9 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU157 | |
| B | GLU157 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:Q8MKF1 |
| Chain | Residue | Details |
| A | ALA2 | |
| B | ALA2 |
