› 1ezr

X-ray diffraction
2.5Å resolution

CRYSTAL STRUCTURE OF NUCLEOSIDE HYDROLASE FROM LEISHMANIA MAJOR

Released:
DOI: 10.2210/pdb1ezr/pdb
PDB entry 1ezr coloured by chain, front view.
PDB entry 1ezr coloured by chain, side view.
PDB entry 1ezr coloured by chain, top view.
Source organism: Leishmania major
Primary publication:
Nucleoside hydrolase from Leishmania major. Cloning, expression, catalytic properties, transition state inhibitors, and the 2.5-å crystal structure.
Shi W, Schramm VL, Almo SC
J Biol Chem 274 21114-20 (1999)
PMID: 10409664

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-160767 (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: 34.31 KDa
Source organism: Leishmania major
Expression system: Escherichia coli
UniProt:
  • Canonical: P83851 (Residues: 1-314; Coverage: 100%)
Gene name: NSNH
Sequence domains: Inosine-uridine preferring nucleoside hydrolase
Structure domains: Ribonucleoside hydrolase-like

Ligands and Environments

1 bound ligand:
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 81.8Å b: 79.2Å c: 109.8Å
α: 90° β: 91.6° γ: 90°
R-values:
R R work R free
0.205 0.203 0.255
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Purine nucleoside phosphorylases: properties, functions, and clinical aspects.
Bzowska et al. (2000)
12 more

12 mentions without citation

Copaifera of the Neotropics: A Review of the Phytochemistry and Pharmacology.
da Trindade et al. (2018)
11 more