› 3p0e

X-ray diffraction
2Å resolution

Structure of hUPP2 in an active conformation with bound 5-benzylacyclouridine

Released:
DOI: 10.2210/pdb3p0e/pdb
PDB entry 3p0e coloured by chain, front view.
PDB entry 3p0e coloured by chain, side view.
PDB entry 3p0e coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A novel structural mechanism for redox regulation of uridine phosphorylase 2 activity.
Roosild TP, Castronovo S, Villoso A, Ziemba A, Pizzorno G
J Struct Biol 176 229-37 (2011)
PMID: 21855639

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131811 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uridine phosphorylase 2 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 297 amino acids
Theoretical weight: 33.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O95045 (Residues: 21-314; Coverage: 93%)
Gene name: UPP2
Sequence domains: Phosphorylase superfamily
Structure domains: Nucleoside phosphorylase domain

Ligands and Environments

2 bound ligands:
Ligand BAU 6 x BAU
Ligand PO4 6 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: C2
Unit cell:
a: 275.342Å b: 56.137Å c: 141.389Å
α: 90° β: 96.38° γ: 90°
R-values:
R R work R free
0.207 0.205 0.242
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Thymidine phosphorylase: A potential new target for treating cardiovascular disease.
Li et al. (2018)
11 other articles

1 mention without citation

A novel structural mechanism for redox regulation of uridine phosphorylase 2 activity.
Roosild et al. (2011)