PDBe 2mas

X-ray diffraction
2.3Å resolution

PURINE NUCLEOSIDE HYDROLASE WITH A TRANSITION STATE INHIBITOR

Released:

Function and Biology Details

Reaction catalysed:
A purine nucleoside + H(2)O = D-ribose + a purine base. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Inosine-uridine preferring nucleoside hydrolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 314 amino acids
Theoretical weight: 34.21 KDa
Source organism: Crithidia fasciculata
Expression system: Escherichia coli
UniProt:
  • Canonical: Q27546 (Residues: 3-315; Coverage: 99%)
Gene name: IUNH
Sequence domains: Inosine-uridine preferring nucleoside hydrolase
Structure domains: Inosine-uridine Nucleoside N-ribohydrolase, chain A

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: I222
Unit cell:
a: 120.63Å b: 159.76Å c: 206.38Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.205 0.234
Expression system: Escherichia coli