6N0U
Crystal structure of a glucose-1-phosphate thymidylyltransferase from Burkholderia phymatum bound to 2'-deoxy-thymidine-B-L-rhamnose
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008879 | molecular_function | glucose-1-phosphate thymidylyltransferase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0008879 | molecular_function | glucose-1-phosphate thymidylyltransferase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0008879 | molecular_function | glucose-1-phosphate thymidylyltransferase activity |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016779 | molecular_function | nucleotidyltransferase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0008879 | molecular_function | glucose-1-phosphate thymidylyltransferase activity |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016779 | molecular_function | nucleotidyltransferase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | binding site for residue TRH A 500 |
| Chain | Residue |
| A | LEU8 |
| A | LEU108 |
| A | ASP110 |
| A | TYR145 |
| A | GLY146 |
| A | GLU161 |
| A | LYS162 |
| A | VAL172 |
| A | THR173 |
| A | GLY174 |
| A | TYR176 |
| A | GLY10 |
| A | ARG194 |
| A | GLU196 |
| A | THR200 |
| A | HOH608 |
| A | HOH651 |
| A | HOH659 |
| A | HOH692 |
| A | HOH706 |
| A | GLY11 |
| A | GLN26 |
| A | GLN82 |
| A | PRO85 |
| A | ASP86 |
| A | GLY87 |
| A | LEU88 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 501 |
| Chain | Residue |
| A | GLY115 |
| A | ASP117 |
| A | LEU118 |
| A | ALA119 |
| A | HOH625 |
| A | HOH686 |
| A | HOH722 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | binding site for residue TRH B 500 |
| Chain | Residue |
| B | LEU8 |
| B | GLY10 |
| B | GLY11 |
| B | GLN26 |
| B | GLN82 |
| B | PRO85 |
| B | ASP86 |
| B | GLY87 |
| B | LEU108 |
| B | ASP110 |
| B | TYR145 |
| B | GLY146 |
| B | GLU161 |
| B | LYS162 |
| B | VAL172 |
| B | THR173 |
| B | GLY174 |
| B | TYR176 |
| B | ARG194 |
| B | GLU196 |
| B | THR200 |
| B | HOH619 |
| B | HOH623 |
| B | HOH639 |
| B | HOH643 |
| B | HOH658 |
| B | HOH683 |
| B | HOH691 |
| B | HOH713 |
| site_id | AC4 |
| Number of Residues | 27 |
| Details | binding site for residue TRH C 500 |
| Chain | Residue |
| C | LEU8 |
| C | GLY10 |
| C | GLY11 |
| C | SER12 |
| C | GLN82 |
| C | PRO85 |
| C | ASP86 |
| C | GLY87 |
| C | LEU108 |
| C | ASP110 |
| C | TYR145 |
| C | GLY146 |
| C | GLU161 |
| C | LYS162 |
| C | VAL172 |
| C | THR173 |
| C | TYR176 |
| C | ARG194 |
| C | GLU196 |
| C | THR200 |
| C | HOH611 |
| C | HOH614 |
| C | HOH616 |
| C | HOH643 |
| C | HOH651 |
| C | HOH668 |
| C | HOH675 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 501 |
| Chain | Residue |
| C | GLY115 |
| C | ASP117 |
| C | LEU118 |
| C | ALA119 |
| C | GLY220 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | binding site for residue TRH D 500 |
| Chain | Residue |
| D | PRO85 |
| D | ASP86 |
| D | GLY87 |
| D | ASP110 |
| D | TYR145 |
| D | GLY146 |
| D | GLU161 |
| D | LYS162 |
| D | VAL172 |
| D | THR173 |
| D | GLY174 |
| D | TYR176 |
| D | ARG194 |
| D | GLU196 |
| D | THR200 |
| D | HOH605 |
| D | HOH607 |
| D | LEU8 |
| D | GLY10 |
| D | GLY11 |
| D | GLN82 |
