› 4nwi

X-ray diffraction
2.05Å resolution

Crystal structure of cytosolic 5'-nucleotidase IIIB (cN-IIIB) bound to cytidine

Released:
DOI: 10.2210/pdb4nwi/pdb
PDB entry 4nwi coloured by chain, front view.
PDB entry 4nwi coloured by chain, side view.
PDB entry 4nwi coloured by chain, top view.
Source organism: Drosophila melanogaster
Primary publication:
Crystal structures of the novel cytosolic 5'-nucleotidase IIIB explain its preference for m7GMP.
Monecke T, Buschmann J, Neumann P, Wahle E, Ficner R
PLoS One 9 e90915 (2014)
PMID: 24603684

Function and Biology Details

Reactions catalysed: 
A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate
CMP + H(2)O = cytidine + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194332 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
7-methylguanosine phosphate-specific 5'-nucleotidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 319 amino acids
Theoretical weight: 36.34 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9W197 (Residues: 1-319; Coverage: 100%)
Gene names: CG3362, cN-IIIB
Sequence domains: Pyrimidine 5'-nucleotidase (UMPH-1)
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 2 x MG
Ligand CTN 2 x CTN
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P21
Unit cell:
a: 46.6Å b: 99.35Å c: 72.81Å
α: 90° β: 92.46° γ: 90°
R-values:
R R work R free
0.228 0.228 0.246
Expression system: Escherichia coli

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Citations

4 review citations

Enzyme promiscuity: engine of evolutionary innovation.
Pandya et al. (2014)
3 more

1 mention without citation

Crystal structures of the novel cytosolic 5'-nucleotidase IIIB explain its preference for m7GMP.
Monecke et al. (2014)