Structure analysis

Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with mutation H309S, crystallized with 2',3'- cyclic AMP

X-ray diffraction
1.9Å resolution
Source organism: Mus musculus
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 11744.91 Å2
Buried surface area: 709.97 Å2
Dissociation area: 293.47 Å2
Dissociation energy (ΔGdiss): -1.19 kcal/mol
Dissociation entropy (TΔSdiss): 4.24 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-147689

Macromolecules

Chain: A
Length: 221 amino acids
Theoretical weight: 24.24 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P16330 (Residues: 179-398; Coverage: 52%)
Gene names: Cnp, Cnp1
Pfam: 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNP or CNPase)
InterPro:
CATH: 2',3'-cyclic nucleotide 3'-phosphodiesterase superfamily

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