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 | 0016779 | molecular_function | nucleotidyltransferase activity |
A | 0045226 | biological_process | extracellular polysaccharide biosynthetic process |
A | 0046872 | molecular_function | metal ion binding |
B | 0008879 | molecular_function | glucose-1-phosphate thymidylyltransferase activity |
B | 0009058 | biological_process | biosynthetic process |
B | 0016779 | molecular_function | nucleotidyltransferase activity |
B | 0045226 | biological_process | extracellular polysaccharide biosynthetic process |
B | 0046872 | molecular_function | metal ion binding |
C | 0008879 | molecular_function | glucose-1-phosphate thymidylyltransferase activity |
C | 0009058 | biological_process | biosynthetic process |
C | 0016779 | molecular_function | nucleotidyltransferase activity |
C | 0045226 | biological_process | extracellular polysaccharide biosynthetic process |
C | 0046872 | molecular_function | metal ion binding |
D | 0008879 | molecular_function | glucose-1-phosphate thymidylyltransferase activity |
D | 0009058 | biological_process | biosynthetic process |
D | 0016779 | molecular_function | nucleotidyltransferase activity |
D | 0045226 | biological_process | extracellular polysaccharide biosynthetic process |
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 |