› 1mas

X-ray diffraction
2.5Å resolution

PURINE NUCLEOSIDE HYDROLASE

Released:
DOI: 10.2210/pdb1mas/pdb
PDB entry 1mas coloured by chain, front view.
PDB entry 1mas coloured by chain, side view.
PDB entry 1mas coloured by chain, top view.
Source organism: Crithidia fasciculata
Primary publication:
Three-dimensional structure of the inosine-uridine nucleoside N-ribohydrolase from Crithidia fasciculata.
Degano M, Gopaul DN, Scapin G, Schramm VL, Sacchettini JC
Biochemistry 35 5971-81 (1996)
PMID: 8634238

Function and Biology Details

Reactions catalysed: 
Inosine + H(2)O = D-ribose + hypoxanthine
Uridine + H(2)O = D-ribose + uracil
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173271 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Inosine-uridine preferring nucleoside hydrolase Chains: A, B
Molecule details ›
Chains: A, B
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: Ribonucleoside hydrolase-like

Ligands and Environments

1 bound ligand:
Ligand K 2 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 63.84Å b: 131.53Å c: 90.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.17 not available
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Catalysis by nucleoside hydrolases.
Versées et al. (2003)
3 more

4 mentions without citation

Ribonucleoside Hydrolases-Structure, Functions, Physiological Role and Practical Uses.
Shaposhnikov et al. (2023)
3 more