› 1tpt

X-ray diffraction
2.8Å resolution

THREE-DIMENSIONAL STRUCTURE OF THYMIDINE PHOSPHORYLASE FROM ESCHERICHIA COLI AT 2.8 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1tpt/pdb
PDB entry 1tpt coloured by chain, front view.
PDB entry 1tpt coloured by chain, side view.
PDB entry 1tpt coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Three-dimensional structure of thymidine phosphorylase from Escherichia coli at 2.8 A resolution.
Walter MR, Cook WJ, Cole LB, Short SA, Koszalka GW, Krenitsky TA, Ealick SE
J Biol Chem 265 14016-22 (1990)
PMID: 2199449

Function and Biology Details

Reaction catalysed: 
Thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139679 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidine phosphorylase Chain: A
Molecule details ›
Chain: A
Length: 440 amino acids
Theoretical weight: 47.24 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P07650 (Residues: 1-440; Coverage: 100%)
Gene names: JW4345, b4382, deoA, tpp, ttg
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 1 x SO4
Ligand TDR 1 x TDR
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P43212
Unit cell:
a: 133Å b: 133Å c: 67.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.28 not available not available
Expression system: Not provided

Quick links

Citations

10 review citations

Functions of the gene products of Escherichia coli.
Riley M. (1993)
9 more

3 mentions without citation

Structures of native human thymidine phosphorylase and in complex with 5-iodouracil.
Mitsiki et al. (2009)
2 more