Function and Biology Details
Reaction catalysed:
Thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Pyrimidine nucleoside phosphorylase, C-terminal
- Pyrimidine nucleoside phosphorylase-like, C-terminal domain superfamily
- Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain superfamily
- Thymidine/pyrimidine-nucleoside phosphorylase
- Pyrimidine-nucleoside phosphorylase, conserved site
- Glycosyl transferase, family 3
- Glycosyl transferase family 3, N-terminal domain
- Pyrimidine-nucleoside phosphorylase, bacterial/eukaryotic
2 more domains
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Thymidine phosphorylase (preferred)
PDBe Complex ID:
PDB-CPX-139679 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidine phosphorylase
Molecule details ›
Chains: A, B
Length: 440 amino acids
Theoretical weight: 47.24 KDa
Source organism: Escherichia coli K-12
UniProt:
Sequence domains:
Length: 440 amino acids
Theoretical weight: 47.24 KDa
Source organism: Escherichia coli K-12
UniProt:
- Canonical:
P07650 (Residues: 1-440; Coverage: 100%)
Sequence domains:
- Glycosyl transferase family, helical bundle domain
- Glycosyl transferase family, a/b domain
- Pyrimidine nucleoside phosphorylase C-terminal domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
RIGAKU RUH3R
Spacegroup:
P21
