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X-ray diffraction
1.9Å resolution

PURINE NUCLEOSIDE PHOSPHORYLASE FROM THERMUS THERMOPHILUS

Released:
DOI: 10.2210/pdb1odk/pdb
PDB entry 1odk coloured by chain, front view.
PDB entry 1odk coloured by chain, side view.
PDB entry 1odk coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Crystal structure of purine nucleoside phosphorylase from Thermus thermophilus.
Tahirov TH, Inagaki E, Ohshima N, Kitao T, Kuroishi C, Ukita Y, Takio K, Kobayashi M, Kuramitsu S, Yokoyama S, Miyano M
J Mol Biol 337 1149-60 (2004)
PMID: 15046984

Function and Biology Details

Reaction catalysed: 
Uridine + phosphate = uracil + alpha-D-ribose 1-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177954 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uridine phosphorylase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 235 amino acids
Theoretical weight: 25.44 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SID9 (Residues: 1-235; Coverage: 100%)
Gene name: TTHA1435
Sequence domains: Phosphorylase superfamily
Structure domains: Nucleoside phosphorylase domain

Ligands and Environments

1 bound ligand:
Ligand GOL 6 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-D
Spacegroup: P43212
Unit cell:
a: 131.919Å b: 131.919Å c: 169.906Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.18 0.208
Expression system: Escherichia coli

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Citations

2 review citations

Survey of the year 2004: literature on applications of isothermal titration calorimetry.
Ababou et al. (2006)
1 more

1 mention without citation

Utilizing molecular docking and cell validation to explore the potential mechanisms of lupenone attenuating the inflammatory response via NF-κB pathway.
Wang et al. (2024)