Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004789 | molecular_function | thiamine-phosphate diphosphorylase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0009228 | biological_process | thiamine biosynthetic process |
A | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE 3NM A 236 |
Chain | Residue |
A | ARG59 |
A | ILE208 |
A | SER209 |
A | IFP237 |
A | HOH263 |
A | HOH264 |
A | HOH277 |
A | HOH441 |
A | HOH450 |
A | GLY151 |
A | PRO152 |
A | THR156 |
A | THR158 |
A | LYS159 |
A | ILE186 |
A | GLY188 |
A | MET207 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE IFP A 237 |
Chain | Residue |
A | TYR29 |
A | ILE31 |
A | GLN57 |
A | ASN92 |
A | HIS107 |
A | SER130 |
A | TYR147 |
A | GLY149 |
A | VAL184 |
A | ILE186 |
A | SER206 |
A | 3NM236 |
A | POP238 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE POP A 238 |
Chain | Residue |
A | ARG59 |
A | LYS61 |
A | ASN92 |
A | ASP93 |
A | GLY109 |
A | ASP112 |
A | SER130 |
A | LYS159 |
A | IFP237 |
A | HOH276 |
A | HOH277 |
A | HOH304 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 9 |
Details | BINDING: |
Chain | Residue | Details |
A | GLN57 | |
A | ASN92 | |
A | ASP93 | |
A | ASP112 | |
A | SER130 | |
A | THR156 | |
A | LYS159 | |
A | GLY188 | |
A | ILE208 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 364 |
Chain | Residue | Details |
A | ARG59 | electrostatic stabiliser |
A | SER130 | electrostatic stabiliser, enhance reactivity |
A | LYS159 | electrostatic stabiliser |