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Biochemical and structural characterization of a divergent loop cyclophilin from Caenorhabditis elegans

X-ray diffraction
1.8Å resolution
PDB entry 1dyw coloured by chain, front view.
PDB entry 1dyw coloured by chain, side view.
PDB entry 1dyw coloured by chain, top view.
Source organism: Caenorhabditis elegans
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Peptidyl-prolyl cis-trans isomerase 3
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Multimeric state: monomeric
Accessible surface area: 7489.59 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-156454

Macromolecules

Peptidyl-prolyl cis-trans isomerase 3
Chain: A
Length: 173 amino acids
Theoretical weight: 18.58 KDa
Source organism: Caenorhabditis elegans
Expression system: Escherichia coli
UniProt:
  • Canonical: P52011 (Residues: 1-173; Coverage: 100%)
Gene names: Y75B12B.5, cyn-3, cyp-3
Pfam: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
InterPro:
CATH: Cyclophilin-like
SCOP: Cyclophilin (peptidylprolyl isomerase)
Peptidyl-prolyl cis-trans isomerase 3 in PDB entry 1dyw, assembly 1, front view.
Peptidyl-prolyl cis-trans isomerase 3 in PDB entry 1dyw, assembly 1, side view.
Peptidyl-prolyl cis-trans isomerase 3 in PDB entry 1dyw, assembly 1, top view.
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