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Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with mutation P225G

X-ray diffraction
2.7Å resolution
PDB entry 4wcc coloured by chain, front view.
PDB entry 4wcc coloured by chain, side view.
PDB entry 4wcc coloured by chain, top view.
Source organism: Mus musculus
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: 2',3'-cyclic-nucleotide 3'-phosphodiesterase
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Multimeric state: monomeric
Accessible surface area: 10875.47 Å2
Buried surface area: 977.88 Å2
Dissociation area: 331.75 Å2
Dissociation energy (ΔGdiss): 4.29 kcal/mol
Dissociation entropy (TΔSdiss): 4.4 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-147689

Macromolecules

2',3'-cyclic-nucleotide 3'-phosphodiesterase
Chain: A
Length: 220 amino acids
Theoretical weight: 24.2 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
2',3'-cyclic-nucleotide 3'-phosphodiesterase in PDB entry 4wcc, assembly 1, front view.
2',3'-cyclic-nucleotide 3'-phosphodiesterase in PDB entry 4wcc, assembly 1, side view.
2',3'-cyclic-nucleotide 3'-phosphodiesterase in PDB entry 4wcc, assembly 1, top view.
PDBe-KB: UniProt Coverage View: P16330  
122020406080100120140160180200220
 
100200
UniProt
P16330
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Early folding residue predictions
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