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Solution NMR

Solution structure of catalytic domain of rat 2',3'-cyclic-nucleotide 3'-phosphodiesterase (CNP) protein

Released:
DOI: 10.2210/pdb2ilx/pdb
PDB entry 2ilx coloured by chain, ensemble of 10 models, front view.
PDB entry 2ilx coloured by chain, ensemble of 10 models, side view.
PDB entry 2ilx coloured by chain, ensemble of 10 models, top view.
Source organism: Rattus norvegicus
Primary publication:
Solution structure of the catalytic domain of RICH protein from goldfish.
Kozlov G, Denisov AY, Pomerantseva E, Gravel M, Braun PE, Gehring K
FEBS J 274 1600-9 (2007)
PMID: 17480208

Function and Biology Details

Reaction catalysed: 
Nucleoside 2',3'-cyclic phosphate + H(2)O = nucleoside 2'-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146516 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2',3'-cyclic-nucleotide 3'-phosphodiesterase Chain: A
Molecule details ›
Chain: A
Length: 219 amino acids
Theoretical weight: 24.25 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P13233 (Residues: 184-398; Coverage: 51%)
Gene names: Cnp, Cnp1
Sequence domains: 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNP or CNPase)
Structure domains: 2',3'-cyclic nucleotide 3'-phosphodiesterase superfamily

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

The myelin membrane-associated enzyme 2',3'-cyclic nucleotide 3'-phosphodiesterase: on a highway to structure and function.
Raasakka et al. (2014)
1 more

1 mention without citation

Myelin 2',3'-cyclic nucleotide 3'-phosphodiesterase: active-site ligand binding and molecular conformation.
Myllykoski et al. (2012)