5IDT
Crystal Structure of a Glucose-1-phosphate Thymidylyltransferase from Burkholderia vietnamiensis with bound Thymidine
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 | 10 |
| Details | binding site for residue THM A 301 |
| Chain | Residue |
| A | LEU9 |
| A | GLU197 |
| A | GLY11 |
| A | GLY12 |
| A | GLN83 |
| A | PRO86 |
| A | ASP87 |
| A | GLY88 |
| A | LEU109 |
| A | ASP111 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| A | GLN91 |
| A | ILE94 |
| A | LEU198 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | PHE151 |
| A | ASN152 |
| A | EDO304 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | ASN152 |
| A | ALA153 |
| A | EDO303 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 301 |
| Chain | Residue |
| B | TRP74 |
| B | GLU255 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue THM D 301 |
| Chain | Residue |
| D | LEU9 |
| D | ALA10 |
| D | GLY11 |
| D | GLN27 |
| D | GLN83 |
| D | PRO86 |
| D | ASP87 |
| D | GLY88 |
| D | LEU89 |
| D | GLY110 |
| D | ASP111 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 302 |
| Chain | Residue |
| D | GLN150 |
| D | PHE151 |
| D | SER169 |
| D | HOH408 |
| D | HOH419 |






